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((short description|Prokaryotic elongation factor))
((Infobox protein family|Symbol=EF-Tu|Name=Elongation Factor Thermo Unstable|image=081-EF-Tu-1ttt.jpg|width=280|caption=EF-Tu (blue) complexed with tRNA (red) and GTP (yellow) <ref>((PDB Molecule of the Month|81|EF-Tu))</ref>|Pfam=GTP_EFTU|Interpro=IPR004541|SCOP=1ETU|CATH=1ETU|InterPro=IPR004541| Pfam_clan = CL0023 | PROSITE = PDOC00273| CDD = cd00881))
((Infobox protein family
| Symbol = GTP_EFTU_D2
| Pfam = PF03144
| Pfam_clan =  
| InterPro = IPR004161
| CDD = cd01342
))
((Infobox protein family
| Symbol = GTP_EFTU_D3
| Name = Elongation factor Tu domain 3
| Pfam = PF03143
| Pfam_clan =  
| InterPro = IPR004160
| CAZy = 
| CDD = cd01513
))
'''EF-Tu''' ('''elongation factor thermo unstable''') is a [[Prokaryotic elongation factors|prokaryotic elongation factor]] responsible for catalyzing the binding of an [[aminoacyl-tRNA]] (aa-tRNA) to the [[ribosome]].  It is a [[G protein|G-protein]], and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome.  As a reflection of its crucial role in [[Translation (biology)|translation]], EF-Tu is one of the most abundant and highly conserved proteins in prokaryotes.<ref>((cite journal | vauthors = Weijland A, Harmark K, Cool RH, Anborgh PH, Parmeggiani A | title = Elongation factor Tu: a molecular switch in protein biosynthesis | journal = Molecular Microbiology | volume = 6 | issue = 6 | pages = 683–8 | date = March 1992 | pmid = 1573997 | doi = 10.1111/j.1365-2958.1992.tb01516.x | doi-access = free ))</ref><ref>((Cite web|url=https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=TIGR00485|title=TIGR00485: EF-Tu|date=March 3, 2017|website=National Center for Biotechnology Information))</ref><ref name=":2">((cite journal | vauthors = Yamamoto H, Qin Y, Achenbach J, Li C, Kijek J, Spahn CM, Nierhaus KH | title = EF-G and EF4: translocation and back-translocation on the bacterial ribosome | journal = Nature Reviews. Microbiology | volume = 12 | issue = 2 | pages = 89–100 | date = February 2014 | pmid = 24362468 | doi = 10.1038/nrmicro3176 | s2cid = 27196901 ))</ref> It is found in eukaryotic mitochondria as [[TUFM]].<ref name="pmid9332382">((cite journal | vauthors = Ling M, Merante F, Chen HS, Duff C, Duncan AM, Robinson BH | title = The human mitochondrial elongation factor tu (EF-Tu) gene: cDNA sequence, genomic localization, genomic structure, and identification of a pseudogene | journal = Gene | volume = 197 | issue = 1–2 | pages = 325–36 |date=Nov 1997 | pmid = 9332382 | doi =10.1016/S0378-1119(97)00279-5  ))</ref>

As a family of elongation factors, EF-Tu also includes its eukaryotic and archaeal homolog, the alpha subunit of [[eEF-1]] (EF-1A).

== Background ==
((see also|Translation (biology)))
Elongation factors are part of the mechanism that synthesizes new [[protein]]s through translation in the ribosome.  [[Transfer RNA]]s (tRNAs) carry the individual [[amino acid]]s that become integrated into a protein sequence, and have an [[anticodon]] for the specific amino acid that they are charged with.  [[Messenger RNA]] (mRNA) carries the genetic information that encodes the [[Protein primary structure|primary structure]] of a protein, and contains [[codons]] that code for each amino acid.  The ribosome creates the protein chain by following the mRNA code and integrating the amino acid of an aminoacyl-tRNA (also known as a charged tRNA) to the growing [[polypeptide]] chain.<ref name=":5">((cite journal | vauthors = Laursen BS, Sørensen HP, Mortensen KK, Sperling-Petersen HU | title = Initiation of protein synthesis in bacteria | journal = Microbiology and Molecular Biology Reviews | volume = 69 | issue = 1 | pages = 101–23 | date = March 2005 | pmid = 15755955 | pmc = 1082788 | doi = 10.1128/MMBR.69.1.101-123.2005 ))</ref><ref name=":6">((cite journal | vauthors = Ramakrishnan V | title = Ribosome structure and the mechanism of translation | journal = Cell | volume = 108 | issue = 4 | pages = 557–72 | date = February 2002 | pmid = 11909526 | doi = 10.1016/s0092-8674(02)00619-0 | s2cid = 2078757 | doi-access = free ))</ref>

There are three sites on the ribosome for tRNA binding.  These are the aminoacyl/acceptor site (abbreviated A), the peptidyl site (abbreviated P), and the exit site (abbreviated E).  The P-site holds the tRNA connected to the polypeptide chain being synthesized, and the A-site is the binding site for a charged tRNA with an anticodon complementary to the mRNA codon associated with the site.  After binding of a charged tRNA to the A-site, a [[peptide bond]] is formed between the growing polypeptide chain on the P-site tRNA and the amino acid of the A-site tRNA, and the entire polypeptide is transferred from the P-site tRNA to the A-site tRNA.  Then, in a process catalyzed by the prokaryotic elongation factor [[EF-G]] (historically known as translocase), the coordinated translocation of the tRNAs and mRNA occurs, with the P-site tRNA moving to the E-site, where it dissociates from the ribosome, and the A-site tRNA moves to take its place in the P-site.<ref name=":5" /><ref name=":6" />

== Biological functions ==
[[File:EF-Tu cycle.png|thumb|The cyclical role of EF-Tu in translation.  Structures are from PDBs [http://www.rcsb.org/pdb/explore/explore.do?structureId=1eft 1EFT], [http://www.rcsb.org/pdb/explore/explore.do?structureId=1tui 1TUI], and [http://www.rcsb.org/pdb/explore/explore.do?structureId=1ttt 1TTT].|left|300x300px]]

=== Protein synthesis ===
EF-Tu participates in the polypeptide elongation process of protein synthesis.  In prokaryotes, the primary function of EF-Tu is to transport the correct aa-tRNA to the A-site of the ribosome.  As a G-protein, it uses [[Guanosine triphosphate|GTP]] to facilitate its function.  Outside of the ribosome, EF-Tu complexed with GTP (EF-Tu • GTP) complexes with aa-tRNA to form a stable EF-Tu • GTP • aa-tRNA [[ternary complex]].<ref name=":3">((cite book | vauthors = Krab IM, Parmeggiani A | title = Mechanisms of EF-Tu, a pioneer GTPase | journal = Progress in Nucleic Acid Research and Molecular Biology | volume = 71 | pages = 513–51 | date = 2002-01-01 | pmid = 12102560 | doi = 10.1016/S0079-6603(02)71050-7 | isbn = 9780125400718 ))</ref>  EF-Tu • GTP binds all correctly-charged aa-tRNAs with approximately identical affinity, except those charged with [[Start codon|initiation residues]] and [[selenocysteine]].<ref>((Cite web|url=http://www.ebi.ac.uk/interpro/entry/IPR004541|title=Translation elongation factor EFTu/EF1A, bacterial/organelle (IPR004541)|website=InterPro))</ref><ref name=":0">((Cite web|url=https://www.rpi.edu/dept/bcbp/molbiochem/MBWeb/mb2/part1/translate.htm|title=Translation: Protein Synthesis|last=Diwan|first=Joyce|date=2008|website=Rensselaer Polytechnic Institute|access-date=2017-03-09|archive-date=2017-06-30|archive-url=https://web.archive.org/web/20170630221049/http://rpi.edu/dept/bcbp/molbiochem/MBWeb/mb2/part1/translate.htm|url-status=dead))</ref>  This can be accomplished because although different amino acid residues have varying [[Side chain#Biochemistry|side-chain]] properties, the tRNAs associated with those residues have varying structures to compensate for differences in side-chain binding affinities.<ref name=":1">((cite journal | vauthors = LaRiviere FJ, Wolfson AD, Uhlenbeck OC | title = Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation | journal = Science | volume = 294 | issue = 5540 | pages = 165–8 | date = October 2001 | pmid = 11588263 | doi = 10.1126/science.1064242 | bibcode = 2001Sci...294..165L | s2cid = 26192336 ))</ref><ref>((cite journal | vauthors = Louie A, Ribeiro NS, Reid BR, Jurnak F | title = Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP | journal = The Journal of Biological Chemistry | volume = 259 | issue = 8 | pages = 5010–6 | date = April 1984 | doi = 10.1016/S0021-9258(17)42947-4 | pmid = 6370998 | doi-access = free ))</ref>

The binding of an aa-tRNA to EF-Tu • GTP allows for the ternary complex to be translocated to the A-site of an active ribosome, in which the anticodon of the tRNA binds to the codon of the mRNA.  If the correct anticodon binds to the mRNA codon, the ribosome changes configuration and alters the geometry of the [[GTPase]] domain of EF-Tu, resulting in the [[hydrolysis]] of the GTP associated with the EF-Tu to [[Guanosine diphosphate|GDP]] and [[Phosphate|Pi]].  As such, the ribosome functions as a [[GTPase-activating protein]] (GAP) for EF-Tu.  Upon GTP hydrolysis, the conformation of EF-Tu changes drastically and dissociates from the aa-tRNA and ribosome complex.<ref name=":2" /><ref name=":4">((cite journal | vauthors = Clark BF, Nyborg J | title = The ternary complex of EF-Tu and its role in protein biosynthesis | journal = Current Opinion in Structural Biology | volume = 7 | issue = 1 | pages = 110–6 | date = February 1997 | pmid = 9032056 | doi = 10.1016/s0959-440x(97)80014-0 ))</ref>  The aa-tRNA then fully enters the A-site, where its amino acid is brought near the P-site's [[polypeptide]] and the ribosome catalyzes the covalent transfer of the polypeptide onto the amino acid.<ref name=":0" />

In the cytoplasm, the deactivated EF-Tu • GDP is acted on by the prokaryotic elongation factor [[EF-Ts]], which causes EF-Tu to release its bound GDP.  Upon dissociation of EF-Ts, EF-Tu is able to complex with a GTP due to the 5– to 10–fold higher concentration of GTP than GDP in the [[cytoplasm]], resulting in reactivated EF-Tu • GTP, which can then associate with another aa-tRNA.<ref name=":3" /><ref name=":4" />

=== Maintaining translational accuracy ===
EF-Tu contributes to translational accuracy in three ways.  In translation, a fundamental problem is that near-cognate anticodons have similar binding affinity to a codon as cognate anticodons, such that anticodon-codon binding in the ribosome alone is not sufficient to maintain high translational fidelity.  This is addressed by the ribosome not activating the GTPase activity of EF-Tu if the tRNA in the ribosome's A-site does not match the mRNA codon, thus preferentially increasing the likelihood for the incorrect tRNA to leave the ribosome.<ref>((cite journal | vauthors = Nilsson J, Nissen P | title = Elongation factors on the ribosome | journal = Current Opinion in Structural Biology | volume = 15 | issue = 3 | pages = 349–54 | date = June 2005 | pmid = 15922593 | doi = 10.1016/j.sbi.2005.05.004 ))</ref>  Additionally, regardless of tRNA matching, EF-Tu also induces a delay after freeing itself from the aa-tRNA, before the aa-tRNA fully enters the A-site (a process called accommodation).  This delay period is a second opportunity for incorrectly charged aa-tRNAs to move out of the A-site before the incorrect amino acid is irreversibly added to the polypeptide chain.<ref>((cite journal |vauthors=Whitford PC, Geggier P, Altman RB, Blanchard SC, Onuchic JN, [[Karissa Sanbonmatsu|Sanbonmatsu KY]] |date=June 2010|title=Accommodation of aminoacyl-tRNA into the ribosome involves reversible excursions along multiple pathways|journal=RNA|volume=16|issue=6|pages=1196–204|doi=10.1261/rna.2035410|pmc=2874171|pmid=20427512))</ref><ref>((cite journal | vauthors = Noel JK, Whitford PC | title = How EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosome | journal = Nature Communications | volume = 7 | pages = 13314 | date = October 2016 | pmid = 27796304 | pmc = 5095583 | doi = 10.1038/ncomms13314 | bibcode = 2016NatCo...713314N ))</ref>  A third mechanism is the less well understood function of EF-Tu to crudely check aa-tRNA associations and reject complexes where the amino acid is not bound to the correct tRNA coding for it.<ref name=":1" />

=== Other functions ===
EF-Tu has been found in large quantities in the [[cytoskeleton]]s of bacteria, co-localizing underneath the [[cell membrane]] with [[MreB]], a cytoskeletal element that maintains cell shape.<ref>((cite journal | vauthors = Defeu Soufo HJ, Reimold C, Linne U, Knust T, Gescher J, Graumann PL | title = Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 7 | pages = 3163–8 | date = February 2010 | pmid = 20133608 | pmc = 2840354 | doi = 10.1073/pnas.0911979107 | doi-access = free | bibcode = 2010PNAS..107.3163D ))</ref><ref>((cite journal | vauthors = Mayer F | title = Cytoskeletons in prokaryotes | journal = Cell Biology International | volume = 27 | issue = 5 | pages = 429–38 | date = 2003-01-01 | pmid = 12758091 | doi = 10.1016/s1065-6995(03)00035-0 | s2cid = 40897586 ))</ref>  Defects in EF-Tu have been shown to result in defects in bacterial morphology.<ref>((cite journal | vauthors = Mayer F | title = Cytoskeletal elements in bacteria Mycoplasma pneumoniae, Thermoanaerobacterium sp., and Escherichia coli as revealed by electron microscopy | journal = Journal of Molecular Microbiology and Biotechnology | volume = 11 | issue = 3–5 | pages = 228–43 | date = 2006-01-01 | pmid = 16983198 | doi = 10.1159/000094057 | s2cid = 23701662 ))</ref>  Additionally, EF-Tu has displayed some [[Chaperone (protein)|chaperone]]-like characteristics, with some experimental evidence suggesting that it promotes the [[Protein folding|refolding]] of a number of [[Denaturation (biochemistry)|denatured]] proteins ''[[in vitro]].''<ref>((cite journal | vauthors = Richarme G | title = Protein-disulfide isomerase activity of elongation factor EF-Tu | journal = Biochemical and Biophysical Research Communications | volume = 252 | issue = 1 | pages = 156–61 | date = November 1998 | pmid = 9813162 | doi = 10.1006/bbrc.1998.9591 ))</ref><ref>((cite journal | vauthors = Kudlicki W, Coffman A, Kramer G, Hardesty B | title = Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing | journal = The Journal of Biological Chemistry | volume = 272 | issue = 51 | pages = 32206–10 | date = December 1997 | pmid = 9405422 | doi = 10.1074/jbc.272.51.32206 | doi-access = free ))</ref>

== Structure ==
[[File:EF-Tu_conformations.png|thumb|480x480px|EF-Tu bound to GDP (yellow) and GDPNP (red), a GTP-like molecule. The GTPase domain (domain I) of EF-Tu is depicted in dark blue, while the oligonucleotide-binding domains II and III are depicted in light blue.  Structures are from PDBs [http://www.rcsb.org/pdb/explore/explore.do?structureId=1eft 1EFT] and [http://www.rcsb.org/pdb/explore/explore.do?structureId=1tui 1TUI], for GDP- and GDPNP-bound EF-Tu, respectively.]]
EF-Tu is a [[monomer]]ic protein with [[molecular weight]] around 43 [[kDa]] in ''[[Escherichia coli]]''.<ref>((cite journal | vauthors = Caldas TD, El Yaagoubi A, Kohiyama M, Richarme G | title = Purification of elongation factors EF-Tu and EF-G from Escherichia coli by covalent chromatography on thiol-sepharose | journal = Protein Expression and Purification | volume = 14 | issue = 1 | pages = 65–70 | date = October 1998 | pmid = 9758752 | doi = 10.1006/prep.1998.0922 ))</ref><ref>((cite journal | vauthors = Wiborg O, Andersen C, Knudsen CR, Clark BF, Nyborg J | title = Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA | journal = The Journal of Biological Chemistry | volume = 271 | issue = 34 | pages = 20406–11 | date = August 1996 | pmid = 8702777 | doi = 10.1074/jbc.271.34.20406 | doi-access = free ))</ref><ref>((cite book | vauthors = Wurmbach P, Nierhaus KH | chapter = Isolation of the protein synthesis elongation factors EF-Tu, EF-Ts, and EF-G from Escherichia coli | title = Nucleic Acids and Protein Synthesis Part H | series = Methods in Enzymology | volume = 60 | pages = [https://archive.org/details/nucleicacids0000unse/page/593 593–606] | date = 1979-01-01 | pmid = 379535 | doi = 10.1016/s0076-6879(79)60056-3 | isbn = 9780121819606 | chapter-url = https://archive.org/details/nucleicacids0000unse/page/593 ))</ref>  The protein consists of three structural [[Protein domain|domains]]: a GTP-binding domain and two [[oligonucleotide]]-binding domains, often referred to as domain 2 and domain 3.  The [[N-terminus|N-terminal]] domain I of EF-Tu is the GTP-binding domain.  It consists of a six [[Beta strand|beta-strand]] core flanked by six [[Alpha helix|alpha-helices]].<ref name=":3" />  Domains II and III of EF-Tu, the oligonucleotide-binding domains, both adopt [[Beta barrel|beta-barrel]] structures.<ref>((cite journal | vauthors = Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB | title = Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus | journal = Nature Structural Biology | volume = 4 | issue = 8 | pages = 650–6 | date = August 1997 | pmid = 9253415 | doi = 10.1038/nsb0897-650 | s2cid = 10644042 ))</ref><ref>((cite journal | vauthors = Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J | title = Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog | journal = Science | volume = 270 | issue = 5241 | pages = 1464–72 | date = December 1995 | pmid = 7491491 | doi = 10.1126/science.270.5241.1464 | s2cid = 24817616 ))</ref>

The GTP-binding domain I undergoes a dramatic conformational change upon GTP hydrolysis to GDP, allowing EF-Tu to dissociate from aa-tRNA and leave the ribosome.<ref>((cite journal | vauthors = Möller W, Schipper A, Amons R | title = A conserved amino acid sequence around Arg-68 of Artemia elongation factor 1 alpha is involved in the binding of guanine nucleotides and aminoacyl transfer RNAs | journal = Biochimie | volume = 69 | issue = 9 | pages = 983–9 | date = September 1987 | pmid = 3126836 | doi = 10.1016/0300-9084(87)90232-x ))</ref>  Reactivation of EF-Tu is achieved by GTP binding in the cytoplasm, which leads to a significant conformational change that reactivates the tRNA-binding site of EF-Tu.  In particular, GTP binding to EF-Tu results in a ~90° rotation of domain I relative to domains II and III, exposing the residues of the tRNA-binding active site.<ref>((cite journal | vauthors = Kjeldgaard M, Nissen P, Thirup S, Nyborg J | title = The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation | journal = Structure | volume = 1 | issue = 1 | pages = 35–50 | date = September 1993 | pmid = 8069622 | doi = 10.1016/0969-2126(93)90007-4 | doi-access = free ))</ref>

Domain 2 adopts a [[beta-barrel]] structure, and is involved in binding to charged tRNA.<ref name="pmid7491491">((cite journal |vauthors=Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J | title = Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog | journal = Science | volume = 270 | issue = 5241 | pages = 1464–72 |date=December 1995 | pmid = 7491491 | doi = 10.1126/science.270.5241.1464| s2cid = 24817616 ))</ref> This domain is [[structurally]] related to the C-terminal domain of [[EF2]], to which it displays weak sequence similarity. This domain is also found in other [[protein]]s such as translation initiation factor [[IF-2]] and [[tetracycline]]-resistance proteins. Domain 3 represents the [[C-terminal]] domain, which adopts a [[beta-barrel]] structure, and is involved in binding to both charged tRNA and to EF1B (or EF-Ts).<ref name="pmid9253415">((cite journal |vauthors=Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB | title = Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus | journal = Nat. Struct. Biol. | volume = 4 | issue = 8 | pages = 650–6 |date=August 1997 | pmid = 9253415 | doi = 10.1038/nsb0897-650| s2cid = 10644042 ))</ref>

=== Evolution ===
((cleanup section|reason=Still terrible, consider just transcluding the section in "further"|date=December 2023))
((further|GTPase#Translation factor family))
The GTP-binding domain is [[conserved sequence|conserved]] in both EF-1alpha/EF-Tu and also in [[EF-2]]/[[EF-G]] and thus seems typical for GTP-dependent proteins which bind non-initiator [[tRNA]]s to the [[ribosome]]. The GTP-binding [[translation factor]] family also includes the [[eukaryotic]] peptide chain [[release factor]] GTP-binding [[protein subunit|subunits]]<ref name="pmid7556078">((cite journal |vauthors=Stansfield I, Jones KM, Kushnirov VV, Dagkesamanskaya AR, Poznyakovski AI, Paushkin SV, Nierras CR, Cox BS, Ter-Avanesyan MD, Tuite MF | title = The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae | journal = EMBO J. | volume = 14 | issue = 17 | pages = 4365–73 |date=September 1995 | pmid = 7556078 | pmc = 394521 | doi = 10.1002/j.1460-2075.1995.tb00111.x))</ref> and [[prokaryotic]] peptide chain release factor 3 (RF-3);<ref name="pmid7737996">((cite journal |vauthors=Grentzmann G, Brechemier-Baey D, Heurgué-Hamard V, Buckingham RH | title = Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGA-containing stop signals | journal = J. Biol. Chem. | volume = 270 | issue = 18 | pages = 10595–600 |date=May 1995 | pmid = 7737996 | doi = 10.1074/jbc.270.18.10595| doi-access = free ))</ref> the [[Prokaryote|prokaryotic]] GTP-binding protein lepA and its [[Homology (biology)|homologue]] in yeast (GUF1) and ''[[Caenorhabditis elegans]]'' (ZK1236.1); [[yeast]] HBS1;<ref name="pmid1394434">((cite journal |vauthors=Nelson RJ, Ziegelhoffer T, Nicolet C, Werner-Washburne M, Craig EA | title = The translation machinery and 70 kd heat shock protein cooperate in protein synthesis | journal = Cell | volume = 71 | issue = 1 | pages = 97–105 |date=October 1992 | pmid = 1394434 | doi = 10.1016/0092-8674(92)90269-I| s2cid = 7417370 ))</ref> [[rat]] Eef1a1 (formerly "statin S1");<ref name="pmid1709933">((cite journal |vauthors=Ann DK, Moutsatsos IK, Nakamura T, Lin HH, Mao PL, Lee MJ, Chin S, Liem RK, Wang E | title = Isolation and characterization of the rat chromosomal gene for a polypeptide (pS1) antigenically related to statin | journal = J. Biol. Chem. | volume = 266 | issue = 16 | pages = 10429–37 |date=June 1991 | doi = 10.1016/S0021-9258(18)99243-4 | pmid = 1709933 | doi-access = free ))</ref> and the [[prokaryote|prokaryotic]] [[selenocysteine]]-specific [[elongation factor]] selB.<ref name="pmid2531290">((cite journal |vauthors=Forchhammer K, Leinfelder W, Bock A | title = Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein | journal = Nature | volume = 342 | issue = 6248 | pages = 453–6 |date=November 1989 | pmid = 2531290 | doi = 10.1038/342453a0 | bibcode = 1989Natur.342..453F | s2cid = 4251625 ))</ref>

== Disease relevance ==
Along with the ribosome, EF-Tu is one of the most important targets for [[Antibiotics|antibiotic]]-mediated inhibition of translation.<ref name=":3" />  Antibiotics targeting EF-Tu can be categorized into one of two groups, depending on the mechanism of action, and one of four structural families.  The first group includes the antibiotics pulvomycin and GE2270A, and inhibits the formation of the ternary complex.<ref>((cite journal | vauthors = Selva E, Beretta G, Montanini N, Saddler GS, Gastaldo L, Ferrari P, Lorenzetti R, Landini P, Ripamonti F, Goldstein BP | title = Antibiotic GE2270 a: a novel inhibitor of bacterial protein synthesis. I. Isolation and characterization | journal = The Journal of Antibiotics | volume = 44 | issue = 7 | pages = 693–701 | date = July 1991 | pmid = 1908853 | doi = 10.7164/antibiotics.44.693 | doi-access = free ))</ref>  The second group includes the antibiotics kirromycin and enacyloxin, and prevents the release of EF-Tu from the ribosome after GTP hydrolysis.<ref>((cite journal | vauthors = Hogg T, Mesters JR, Hilgenfeld R | title = Inhibitory mechanisms of antibiotics targeting elongation factor Tu | journal = Current Protein & Peptide Science | volume = 3 | issue = 1 | pages = 121–31 | date = February 2002 | pmid = 12370016 | doi = 10.2174/1389203023380855 ))</ref><ref>((cite journal | vauthors = Andersen GR, Nissen P, Nyborg J | title = Elongation factors in protein biosynthesis | journal = Trends in Biochemical Sciences | volume = 28 | issue = 8 | pages = 434–41 | date = August 2003 | pmid = 12932732 | doi = 10.1016/S0968-0004(03)00162-2 ))</ref><ref>((cite journal | vauthors = Parmeggiani A, Nissen P | title = Elongation factor Tu-targeted antibiotics: four different structures, two mechanisms of action | journal = FEBS Letters | volume = 580 | issue = 19 | pages = 4576–81 | date = August 2006 | pmid = 16876786 | doi = 10.1016/j.febslet.2006.07.039 | s2cid = 20811259 | doi-access = free ))</ref>

== See also ==
* [[Prokaryotic elongation factors]]
* [[EF-Ts]] (elongation factor thermo stable)
* [[EF-G]] (elongation factor G)
* [[Elongation factor P|EF-P]] (elongation factor P) 
* [[eEF-1]] 
* [[EFR (EF-Tu receptor)]]

== References ==
((Reflist|32em))

== External links ==
* ((MeshName|Peptide+Elongation+Factor+Tu))
* ((PDBe-KB2|P49410|Elongation factor Tu, mitochondrial))

((InterPro content|IPR000795|IPR004161|IPR004160))

((GeneticTranslation))
((GTPases))

[[Category:Protein biosynthesis]]
[[Category:Protein domains]]

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