PF13581

Histidine kinase-like ATPase domain

Pfam entry
Member databasePfam
Pfam typedomain
Short nameHATPase_c_2
ClanHis_Kinase_A
Author Bateman A;0000-0002-6982-4660
Sequence Ontology0000417

Description
Imported from IPR003594

This domain is found in several ATP-binding proteins, including: histidine kinase
[5]
, DNA gyrase B, topoisomerases
[4]
, heat shock protein HSP90
[1, 3, 2]
, phytochrome-like ATPases and DNA mismatch repair proteins. The fold of this domain consists of two layers, α/β, which contains an 8-stranded mixed β-sheet.

References
Imported from IPR003594

1.Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT. J. Biol. Chem. 279, 46162-71, (2004). View articlePMID: 15292259

2.Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. 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. Chem. Biol. 11, 775-85, (2004). View articlePMID: 15217611

3.The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH. Cell 116, 87-98, (2004). View articlePMID: 14718169

4.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. Bellon S, Parsons JD, Wei Y, Hayakawa K, Swenson LL, Charifson PS, Lippke JA, Aldape R, Gross CH. Antimicrob. Agents Chemother. 48, 1856-64, (2004). View articlePMID: 15105144

5.Crystal structure of the C-terminal domain of the two-component system transmitter protein nitrogen regulator II (NRII; NtrB), regulator of nitrogen assimilation in Escherichia coli. Song Y, Peisach D, Pioszak AA, Xu Z, Ninfa AJ. Biochemistry 43, 6670-8, (2004). View articlePMID: 15157101

Wikipedia

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.