1E59

E.coli cofactor-dependent phosphoglycerate mutase complexed with vanadate

1E59 の概要

• エントリーDOI: 10.2210/pdb1e59/pdb
• 関連するPDBエントリー: 1E58
• 分子名称: PHOSPHOGLYCERATE MUTASE, TETRAMETAVANADATE, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: inhibitor, vandate, glycolysis and gluconeogenesis, phosphoglycerate mutase, isomerase
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28912.41

構造登録者

Bond, C.S.,Hunter, W.N. (登録日: 2000-07-19, 公開日: 2002-02-05, 最終更新日: 2023-12-13)

主引用文献

Bond, C.S.,White, M.,Hunter, W.N.
Mechanistic Implications for Escherichia Coli Cofactor-Dependent Phosphoglycerate Mutase Based on the High-Resolution Crystal Structure of a Vanadate Complex.
J.Mol.Biol., 316:1071-, 2002

PubMed Abstract: The structure of Escherichia coli cofactor-dependent phosphoglycerate mutase (dPGM), complexed with the potent inhibitor vanadate, has been determined to a resolution of 1.30 A (R-factor 0.159; R-free 0.213). The inhibitor is present in the active site, principally as divanadate, but with evidence of additional vanadate moieties at either end, and representing a different binding mode to that observed in the structural homologue prostatic acid phosphatase. The analysis reveals the enzyme-ligand interactions involved in inhibition of the mutase activity by vanadate and identifies a water molecule, observed in the native E.coli dPGM structure which, once activated by vanadate, may dephosphorylate the active protein. Rather than reflecting the active conformation previously observed for E.coli dPGM, the inhibited protein's conformation resembles that of the inactive dephosphorylated Saccharomyces cerevisiae dPGM. The provision of a high-resolution structure of both active and inactive forms of dPGM from a single organism, in conjunction with computational modelling of substrate molecules in the active site provides insight into the binding of substrates and the specific interactions necessary for three different activities, mutase, synthase and phosphatase, within a single active site. The sequence similarity of E.coli and human dPGMs allows us to correlate structure with clinical pathology.

PubMed: 11884145
DOI: 10.1006/JMBI.2002.5418

実験手法

X-RAY DIFFRACTION (1.3 Å)