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PDBsum entry 1ngc

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Hydrolase(acting on acid anhydrides) PDB id
1ngc
Contents
Protein chain
378 a.a.
Ligands
PO4
ADP
Metals
_MG
Waters ×141

References listed in PDB file
Key reference
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
The ATPase fragment of the bovine 70-kDa heat shock cognate protein is an attractive construct in which to study its mechanism of ATP hydrolysis. The three-dimensional structure suggests several residues that might participate in the ATPase reaction. Four acidic residues (Asp-10, Glu-175, Asp-199, and Asp-206) have been individually mutated to both the cognate amine (asparagine/glutamine) and to serine, and the effects of the mutations on the kinetics of the ATPase activity (Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) J. Biol. Chem. 269, 12893-12898) and the structure of the mutant ATPase fragments have been determined, typically to approximately 2.4 A resolution. Additionally, the structures of the wild type protein complexed with MgADP and Pi, MgAMPPNP (5'-adenylyl-beta, gamma-imidodiphosphate) and CaAMPPNP have been refined to 2.1, 2.4, and 2.4 A, respectively. Combined, these structures provide models for the prehydrolysis, MgATP-bound state and the post-hydrolysis, MgADP-bound state of the ATPase fragment. These models suggest a pathway for the hydrolytic reaction in which 1) the gamma phosphate of bound ATP reorients to form a beta, gamma-bidentate phosphate complex with the Mg2+ ion, allowing 2) in-line nucleophilic attack on the gamma phosphate by a H2O molecule or OH- ion, with 3) subsequent release of inorganic phosphate.
Secondary reference #1
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.
PubMed id 2143562
Abstract
PROCHECK
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