1HPM

HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE

1HPM の概要

• エントリーDOI: 10.2210/pdb1hpm/pdb
• 分子名称: 44K ATPASE FRAGMENT (N-TERMINAL) OF 7O kD HEAT-SHOCK COGNATE PROTEIN, MAGNESIUM ION, PHOSPHATE ION, ... (7 entities in total)
• 機能のキーワード: hydrolase (acting on acid anhydrides)
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43208.61

構造登録者

Wilbanks, S.M.,Mckay, D.B. (登録日: 1995-03-24, 公開日: 1995-07-31, 最終更新日: 2024-02-07)

主引用文献

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

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: 7836458
DOI: 10.1074/jbc.270.5.2251

実験手法

X-RAY DIFFRACTION (1.7 Å)