2ie8
From Proteopedia
|
Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation
Overview
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.
About this Structure
2IE8 is a Single protein structure of sequence from Thermus caldophilus. Active as Phosphoglycerate kinase, with EC number 2.7.2.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation., Lee JH, Im YJ, Bae J, Kim D, Kim MK, Kang GB, Lee DS, Eom SH, Biochem Biophys Res Commun. 2006 Dec 1;350(4):1044-9. Epub 2006 Oct 6. PMID:17045964
Page seeded by OCA on Wed Nov 21 12:16:33 2007
