2IE8

Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation

2IE8 の概要

• エントリーDOI: 10.2210/pdb2ie8/pdb
• 分子名称: phosphoglycerate kinase (2 entities in total)
• 機能のキーワード: domain movement, phosphoglycerate kinase, thermus caldophilus, transferase
• 由来する生物種: Thermus caldophilus
• 細胞内の位置: Cytoplasm (By similarity): Q08GC7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41804.90

構造登録者

Lee, J.H.,Im, Y.J.,Eom, S.H. (登録日: 2006-09-18, 公開日: 2006-11-07, 最終更新日: 2023-10-25)

主引用文献

Lee, J.H.,Im, Y.J.,Bae, J.,Kim, D.,Kim, M.K.,Kang, G.B.,Lee, D.S.,Eom, S.H.
Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation
Biochem.Biophys.Res.Commun., 350:1044-1049, 2006

PubMed Abstract: Phosphoglycerate kinase (PGK) is a key glycolytic enzyme that catalyzes the reversible transfer of a phosphate from 1,3-bisphosphoglycerate to ADP to form 3-phosphoglycerate and ATP in the presence of magnesium. During catalysis, a conformational change occurs that brings the N- and C-domains of PGK closer together. Here we present the 1.8A crystal structure of unliganded PGK from Thermus caldophilus (Tca). Comparison of the structure of TcaPGK (open conformation) with that of Thermotoga maritima (Tma) PGK (closed conformation) revealed that the conformational change reflects a change in the interaction between the domains. We identified Arg148 as a key residue involved in open-to-closed transition. The open conformation of TcaPGK is stabilized by an interdomain salt bridge between Arg148 and Glu375. The binding of 3-PG (or maybe 1,3-BPG) disrupts this salt bridge and, in ternary complex, the formation of new salt bridge between Arg60 and Asp197 stabilizes the closed conformation.

PubMed: 17045964
DOI: 10.1016/j.bbrc.2006.09.151

実験手法

X-RAY DIFFRACTION (1.8 Å)