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PDBsum entry 1ngc
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Hydrolase(acting on acid anhydrides)
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PDB id
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1ngc
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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K.M.Flaherty,
S.M.Wilbanks,
C.Deluca-Flaherty,
D.B.Mckay.
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Ref.
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J Biol Chem, 1994,
269,
12899-12907.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Three-Dimensional structure of the atpase fragment of a 70k heat-Shock cognate protein.
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Authors
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K.M.Flaherty,
C.Deluca-Flaherty,
D.B.Mckay.
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Ref.
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Nature, 1990,
346,
623-628.
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PubMed id
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