Reference: Wilbanks SM and McKay DB (1995) How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J Biol Chem 270(5):2251-7

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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.

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Journal Article | Research Support, U.S. Gov't, P.H.S.
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Wilbanks SM, McKay DB
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