1YJX

Crystal structure of human B type phosphoglycerate mutase

1YJX の概要

• エントリーDOI: 10.2210/pdb1yjx/pdb
• 関連するPDBエントリー: 1YFK
• 分子名称: Phosphoglycerate mutase 1, CHLORIDE ION, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: alpha/beta, isomerase, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 361523.45

構造登録者

Wang, Y.,Wei, Z.,Liu, L.,Gong, W. (登録日: 2005-01-16, 公開日: 2005-05-17, 最終更新日: 2023-10-25)

主引用文献

Wang, Y.,Wei, Z.,Liu, L.,Cheng, Z.,Lin, Y.,Ji, F.,Gong, W.
Crystal structure of human B-type phosphoglycerate mutase bound with citrate.
Biochem.Biophys.Res.Commun., 331:1207-1215, 2005

PubMed Abstract: The B-type cofactor-dependent phosphoglycerate mutase (dPGM-B) catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in glycolysis and gluconeogenesis pathways using 2,3-bisphosphoglycerate as the cofactor. The crystal structures of human dPGM-B bound with citrate were determined in two crystal forms. These structures reveal a dimerization mode conserved in both of dPGM and BPGM (bisphosphoglycerate mutase), based on which a dPGM/BPGM heterodimer structure is proposed. Structural comparison supports that the conformational changes of residues 13-21 and 98-117 determine PGM/BPGM activity differences. The citrate-binding mode suggests a substrate-binding model, consistent with the structure of Escherichia coli dPGM/vanadate complex. A chloride ion was found in the center of the dimer, providing explanation for the contribution of chloride ion to dPGM activities. Based on the structural information, the possible reasons for the deficient human dPGM mutations found in some patients are also discussed.

PubMed: 15883004
DOI: 10.1016/j.bbrc.2005.03.243

実験手法

X-RAY DIFFRACTION (2.8 Å)