Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase

Andrea Varga, Beáta Flachner, Peter Konarev, Éva Gráczer, Judit Szabó, Dmitri Svergun, Péter Závodszky, Mária Vas

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Closure of the two domains of 3-phosphoglycerate kinase, upon substrate binding, is essential for the enzyme function. The available crystal structures cannot provide sufficient information about the mechanism of substrate assisted domain closure and about the requirement of only one or both substrates, since lattice forces may hinder the large scale domain movements. In this study the known X-ray data, obtained for the open and closed conformations, were probed by solution small-angle X-ray scattering experiments. The results prove that binding of both substrates is essential for domain closure. Molecular graphical analysis, indeed, reveals formation of a double-sided H-bond network, which affects substantially the shape of the main molecular hinge at β-strand L, under the concerted action of both substrates.

Original languageEnglish
Pages (from-to)2698-2706
Number of pages9
JournalFEBS letters
Volume580
Issue number11
DOIs
Publication statusPublished - May 15 2006

Keywords

  • Domain movement
  • Main hinge
  • Phosphoglycerate kinase
  • Small-angle X-ray scattering
  • Substrate effects

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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