GHKL domain

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Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
PDB 1ah6 EBI.jpg
Structure of the N-terminal domain of the yeast Hsp90 chaperone.[1]
Identifiers
SymbolHATPase_c
PfamPF02518
InterProIPR003594
SMARTHATPase_c
SCOP1ei1
SUPERFAMILY1ei1
CDDcd00075
 
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Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
PDB 1ah6 EBI.jpg
Structure of the N-terminal domain of the yeast Hsp90 chaperone.[1]
Identifiers
SymbolHATPase_c
PfamPF02518
InterProIPR003594
SMARTHATPase_c
SCOP1ei1
SUPERFAMILY1ei1
CDDcd00075

The GHKL domain (Gyrase, Hsp90, Histidine Kinase, MutL) is an evolutionary conserved protein domain.[2]

This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90. This domain is found in several ATP-binding proteins for example: 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]

Subfamilies[edit]

Members[edit]

References[edit]

  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. 
  2. ^ 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. 
  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