1HPM
HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE
Summary for 1HPM
| Entry DOI | 10.2210/pdb1hpm/pdb |
| Descriptor | 44K ATPASE FRAGMENT (N-TERMINAL) OF 7O kD HEAT-SHOCK COGNATE PROTEIN, MAGNESIUM ION, PHOSPHATE ION, ... (7 entities in total) |
| Functional Keywords | hydrolase (acting on acid anhydrides) |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 43208.61 |
| Authors | Wilbanks, S.M.,Mckay, D.B. (deposition date: 1995-03-24, release date: 1995-07-31, Last modification date: 2024-02-07) |
| Primary citation | Wilbanks, S.M.,McKay, D.B. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J.Biol.Chem., 270:2251-2257, 1995 Cited by PubMed 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. PubMed: 7836458DOI: 10.1074/jbc.270.5.2251 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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