2H4Z

Human bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerate

2H4Z の概要

• エントリーDOI: 10.2210/pdb2h4z/pdb
• 関連するPDBエントリー: 2H4X 2H52
• 分子名称: Bisphosphoglycerate mutase, (2R)-2,3-diphosphoglyceric acid (3 entities in total)
• 機能のキーワード: bisphosphoglycerate mutase, 2, 3-bisphosphoglycerate, isomerase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62768.82

構造登録者

Wang, Y.,Gong, W. (登録日: 2006-05-25, 公開日: 2006-10-24, 最終更新日: 2023-10-25)

主引用文献

Wang, Y.,Liu, L.,Wei, Z.,Cheng, Z.,Lin, Y.,Gong, W.
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.
J.Biol.Chem., 281:39642-39648, 2006

PubMed Abstract: Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin. In this paper, we directly observed real-time motion of the enzyme active site and the substrate during phosphoryl transfer. A series of high resolution crystal structures of human bisphosphoglycerate mutase co-crystallized with 2,3-bisphosphoglycerate, representing different time points in the phosphoryl transfer reaction, were solved. These structures not only clarify the argument concerning the substrate binding mode for this enzyme family but also depict the entire process of the key histidine phosphorylation as a "slow movie". It was observed that the enzyme conformation continuously changed during the different states of the reaction. These results provide direct evidence for an "in line" phosphoryl transfer mechanism, and the roles of some key residues in the phosphoryl transfer process are identified.

PubMed: 17052986
DOI: 10.1074/jbc.M606421200

実験手法

X-RAY DIFFRACTION (2 Å)