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Title 

Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation

Authors 

J H LeeY J ImJungdon BaeDooil KimM K KimG B KangDae Sil LeeS H Eom

Publisher 

Elsevier

Issue Date 

2006

Citation 

Biochemical and Biophysical Research Communications, vol. 350, no. 4, pp. 1044-1049

Keywords 

crystal structuredomain movementphosphoglycerate kinasethermus caldophilusconformational transitionprotein conformationcrystallographythermus

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 1.8 ? 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.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2006.09.151

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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