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PDBsum entry 1hpm

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Hydrolase (acting on acid anhydrides) PDB id
1hpm
Jmol
Contents
Protein chain
378 a.a.
Ligands
PO4
ADP
Metals
_MG
__K ×2
_CL ×2
Waters ×429

References listed in PDB file
Key reference
Title How potassium affects the activity of the molecular chaperone hsc70. Ii. Potassium binds specifically in the atpase active site.
Authors S.M.Wilbanks, D.B.Mckay.
Ref. J Biol Chem, 1995, 270, 2251-2257.
PubMed id 7836458
Abstract
Crystallographic anomalous scattering from potassium at 1.7 A resolution reveals two monovalent ions that interact with MgADP and P(i) in the nucleotide binding cleft of wild-type recombinant bovine Hsc70 ATPase fragment. K+ at site 1 interacts with oxygens of the beta-phosphate of ADP, whereas K+ at site 2 interacts with an oxygen of P(i). Both K+ ions also interact with specific H2O molecules in the first hydration shell of the octahedrally coordinated Mg2+ ion and with specific protein ligands. In crystals that have Na+ present, K+ is replaced by a Na+ ion at site 1 and by a Na(+)-H2O pair at site 2. The K+ ions are positioned where they could stabilize binding of a beta,gamma-bidentate MgATP complex with Hsc70, as well as a transition state during ATP hydrolysis, suggesting that monovalent ions act as specific metal cofactors in the ATPase reaction of Hsc70.
Secondary reference #1
Title How potassium affects the activity of the molecular chaperone hsc70. I. Potassium is required for optimal atpase activity.
Authors M.C.O'Brien, D.B.Mckay.
Ref. J Biol Chem, 1995, 270, 2247-2250.
PubMed id 7836457
Abstract
Secondary reference #2
Title Structural basis of the 70-Kilodalton heat shock cognate protein atp hydrolytic activity. Ii. Structure of the active site with adp or atp bound to wild type and mutant atpase fragment.
Authors K.M.Flaherty, S.M.Wilbanks, C.Deluca-Flaherty, D.B.Mckay.
Ref. J Biol Chem, 1994, 269, 12899-12907.
PubMed id 8175707
Abstract
Secondary reference #3
Title Three-Dimensional structure of the atpase fragment of a 70k heat-Shock cognate protein.
Authors K.M.Flaherty, C.Deluca-Flaherty, D.B.Mckay.
Ref. Nature, 1990, 346, 623-628. [DOI no: 10.1038/346623a0]
PubMed id 2143562
Abstract
PROCHECK
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