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PDBsum entry 1hpm
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Hydrolase (acting on acid anhydrides)
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PDB id
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1hpm
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References listed in PDB file
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Key reference
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Title
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How potassium affects the activity of the molecular chaperone hsc70. Ii. Potassium binds specifically in the atpase active site.
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Authors
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S.M.Wilbanks,
D.B.Mckay.
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Ref.
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J Biol Chem, 1995,
270,
2251-2257.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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How potassium affects the activity of the molecular chaperone hsc70. I. Potassium is required for optimal atpase activity.
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Authors
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M.C.O'Brien,
D.B.Mckay.
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Ref.
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J Biol Chem, 1995,
270,
2247-2250.
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PubMed id
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Secondary reference #2
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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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Secondary reference #3
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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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