4CSM

YEAST CHORISMATE MUTASE + TYR + ENDOOXABICYCLIC INHIBITOR

4CSM の概要

• エントリーDOI: 10.2210/pdb4csm/pdb
• 分子名称: CHORISMATE MUTASE, TYROSINE, 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID (3 entities in total)
• 機能のキーワード: chorismate pyruvate mutase, allosteric protein, complex (isomerase-peptide), transition state analog, complex (isomerase-peptide) complex, complex (isomerase/peptide)
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60397.12

構造登録者

Straeter, N.,Schnappauf, G.,Braus, G.,Lipscomb, W.N. (登録日: 1997-07-14, 公開日: 1998-01-14, 最終更新日: 2024-05-22)

主引用文献

Strater, N.,Schnappauf, G.,Braus, G.,Lipscomb, W.N.
Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures.
Structure, 5:1437-1452, 1997

PubMed Abstract: Chorismate mutase (CM) catalyzes the Claisen rearrangement of chorismate to prephenate, notably the only known enzymatically catalyzed pericyclic reaction in primary metabolism. Structures of the enzyme in complex with an endo-oxabicyclic transition state analogue inhibitor, previously determined for Bacillus subtilis and Escherichia coli CM, provide structural insight into the enzyme mechanism. In contrast to these bacterial CMs, yeast CM is allosterically regulated in two ways: activation by tryptophan and inhibition by tyrosine. Yeast CM exists in two allosteric states, R (active) and t (inactive).

PubMed: 9384560
DOI: 10.1016/S0969-2126(97)00294-3

実験手法

X-RAY DIFFRACTION (2.8 Å)