4NWX

Crystal structure of phosphoglycerate mutase from Staphylococcus aureus in 2-phosphoglyceric acid bound form

4NWX の概要

• エントリーDOI: 10.2210/pdb4nwx/pdb
• 関連するPDBエントリー: 4NWJ
• 分子名称: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, 2-PHOSPHOGLYCERIC ACID, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: isomerase, glycolytic enzyme, cytosol
• 由来する生物種: Staphylococcus aureus subsp. aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57910.99

構造登録者

Roychowdhury, A.,Kundu, A.,Bose, M.,Gujar, A.,Das, A.K. (登録日: 2013-12-07, 公開日: 2015-01-14, 最終更新日: 2023-11-08)

主引用文献

Roychowdhury, A.,Kundu, A.,Bose, M.,Gujar, A.,Mukherjee, S.,Das, A.K.
Complete catalytic cycle of cofactor-independent phosphoglycerate mutase involves a spring-loaded mechanism
Febs J., 282:1097-1110, 2015

PubMed Abstract: Cofactor-independent phosphoglycerate mutase (iPGM), an important enzyme in glycolysis and gluconeogenesis, catalyses the isomerization of 2- and 3-phosphoglycerates by an Mn(2+)-dependent phospho-transfer mechanism via a phospho-enzyme intermediate. Crystal structures of bi-domain iPGM from Staphylococcus aureus, together with substrate-bound forms, have revealed a new conformation of the enzyme, representing an intermediate state of domain movement. The substrate-binding site and the catalytic site are present in two distinct domains in the intermediate form. X-ray crystallography complemented by simulated dynamics has enabled delineation of the complete catalytic cycle, which includes binding of the substrate, followed by its positioning into the catalytic site, phospho-transfer and finally product release. The present work describes a novel mechanism of domain movement controlled by a hydrophobic patch that is exposed on domain closure and acts like a spring to keep the protein in open conformation. Domain closing occurs after substrate binding, and is essential for phospho-transfer, whereas the open conformation is a prerequisite for efficient substrate binding and product dissociation. A new model of catalysis has been proposed by correlating the hinge-bending motion with the phospho-transfer mechanism.

PubMed: 25611430
DOI: 10.1111/febs.13205

実験手法

X-RAY DIFFRACTION (2.01 Å)