Insight into the mechanism of domain movements and its role in functioning of 3-phosphoglycerate kinase

M. Vas, A. Varga, J. Szabo, E. Graczer, B. Flachner, P. Zavodszky, P. Konarev, D. Svergun

Research output: Contribution to journalArticle

Abstract

Comprehensive studies with 3-phosphoglycerate kinase revealed the details of transmission of a substrate-triggered conformational effect towards the main molecular hinge at the β-strand L. The unusual kinetic behavior (activation by anions) and flexibility of the phosphate chain of the nucleotide substrate(s) can be related to domain movements. Both phenomena are due to interactions with the catalytic Lys residue, which moves more than 10 Å during domain closure. This movement occurs, in concert with operation of the main hinge, under the simultaneous action of the two substrates.

Original languageEnglish
Pages (from-to)114-119
Number of pages6
JournalMoscow University Chemistry Bulletin
Volume63
Issue number2
DOIs
Publication statusPublished - Apr 2008

ASJC Scopus subject areas

  • Chemistry(all)

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