Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure of the N-terminal domain of the yeast Hsp90 chaperone.[1]
Identifiers
SymbolHATPase_c
PfamPF02518
InterProIPR003594
SMARTHATPase_c
SCOP21ei1 / SCOPe / SUPFAM
CDDcd00075
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1ys3B:338-445 1ysrB:338-445 1id0A:374-479

2c2aA:365-479 1i58A:398-540 1b3qB:398-540 1i5bA:398-540 1i5aB:398-540 1i5dA:398-540 1i5cB:398-540 1i59B:398-540 1y8nA:236-361 1y8oA:236-361 1y8pA:236-361 1jm6A:240-363 1gkxA:264-403 1gkzA:264-403 1gjvA:264-403 1nhjA:18-79 1nhiA:18-79 1nhhA:18-79 1b62A:18-79 1bknB:20-73 1b63A:18-79 1h7sA:30-164 1h7uA:30-164 1ea6B:30-164 1mx0D:27-179 1mu5A:27-179 1z5bA:27-179 1z5cB:27-179 1z59A:27-179 1z5aB:27-179 1thnC:35-136 1tidC:35-136 1l0oA:35-136 1tilE:35-136 1th8A:35-136 1ah6 :26-180 1us7A:26-180 1amw :26-180 2breA:26-180 2akpB:26-180 1a4h :26-180 1ah8A:26-180 2brcA:26-180 1am1 :26-180 1bgqA:26-180 1yc4A:40-193 1uygA:40-193 2bt0A:40-193 1uycA:40-193 1yer :40-193 1yc3A:40-193 1uy8A:40-193 2bz5A:40-193 1uyeA:40-193 2byhA:40-193 1yc1A:40-193 1uyhA:40-193 1uy9A:40-193 1uydA:40-193 1uy6A:40-193 1uy7A:40-193 2bsmA:40-193 1yes :40-193 1uylA:40-193 1uyiA:40-193 2byiA:40-193 1uyfA:40-193 1byqA:40-193 1uykA:40-193 1osfA:40-193 1yet :40-193 1uymA:35-188 1tc0B:96-254 1yszA:96-254 1u2oB:96-254 1yt0A:96-254 1tbwA:96-254 1qyeA:96-254 1u0zA:96-254 1yt2A:96-254 1tc6A:96-254 1u0yA:96-254 1qy8A:96-254 1yt1A:96-254 1qy5A:96-254 1y4uB:27-183 1y4sA:27-183 1kijA:28-173 1s16A:27-172 1s14B:27-172 1pvgA:55-204 1qzrB:55-204 1zxnC:76-224

1zxmA:76-224

The GHKL domain (Gyrase, Hsp90, Histidine Kinase, MutL) is an evolutionary conserved protein domain.[2] It is an ATPase domain found in several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases,[3] heat shock protein HSP90,[4][5][6] phytochrome-like ATPases and DNA mismatch repair proteins.

More information about this protein can be found at Protein of the Month: DNA Topoisomerase.[7]

Structure

The fold of this domain consists of two layers, alpha/beta, which contain an 8-stranded mixed beta-sheet.[2]

Subfamilies

InterPro: IPR020575

InterPro: IPR032834

Members

References

  1. ^ Prodromou C, Roe SM, Piper PW, Pearl LH (June 1997). "A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone". Nat. Struct. Biol. 4 (6): 477–82. doi:10.1038/nsb0697-477. PMID 9187656. S2CID 38764610.
  2. ^ a b Dutta R, Inouye M (January 2000). "GHKL, an emergent ATPase/kinase superfamily". Trends Biochem. Sci. 25 (1): 24–8. doi:10.1016/S0968-0004(99)01503-0. PMID 10637609.
  3. ^ Bellon S, Parsons JD, Wei Y, Hayakawa K, Swenson LL, Charifson PS, Lippke JA, Aldape R, Gross CH (May 2004). "Crystal Structures of Escherichia coli Topoisomerase IV ParE Subunit (24 and 43 Kilodaltons): a Single Residue Dictates Differences in Novobiocin Potency against Topoisomerase IV and DNA Gyrase". Antimicrob. Agents Chemother. 48 (5): 1856–64. doi:10.1128/AAC.48.5.1856-1864.2004. PMC 400558. PMID 15105144.
  4. ^ Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT (October 2004). "Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone". J. Biol. Chem. 279 (44): 46162–71. doi:10.1074/jbc.M405253200. PMID 15292259.
  5. ^ Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH (January 2004). "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell. 116 (1): 87–98. doi:10.1016/S0092-8674(03)01027-4. PMID 14718169. S2CID 797232.
  6. ^ Wright L, Barril X, Dymock B, Sheridan L, Surgenor A, Beswick M, Drysdale M, Collier A, Massey A, Davies N, Fink A, Fromont C, Aherne W, Boxall K, Sharp S, Workman P, Hubbard RE (June 2004). "Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms". Chem. Biol. 11 (6): 775–85. doi:10.1016/j.chembiol.2004.03.033. PMID 15217611.
  7. ^ McDowall J (2006). "DNA Topoisomerase". Protein of the month. InterPro.
This article incorporates text from the public domain Pfam and InterPro: IPR003594


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