Role of side-chains in the operation of the main molecular hinge of 3-phosphoglycerate kinase

Judit Szabó, Andrea Varga, Beáta Flachner, Peter V. Konarev, Dmitri I. Svergun, Péter Závodszky, Mária Vas

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The single mutants (F165A, E192A, F196A, S392A, T393A) at and near the main hinge (β-strand L) of human 3-phosphoglycerate kinase (hPGK) exhibit variously reduced enzyme activity, indicating the cumulative effects of these residues in regulating domain movements. The residues F165 and E192 are also essential in maintaining the conformational integrity of the whole molecule, including the hinge-region. Shortening of βL by deleting T393 has led to a dramatic activity loss and the concomitant absence of domain closure (as detected by small angle X-ray scattering), demonstrating the role of βL in functioning of hPGK. The role of each residue in the conformational transmission is described.

Original languageEnglish
Pages (from-to)1335-1340
Number of pages6
JournalFEBS letters
Volume582
Issue number9
DOIs
Publication statusPublished - Apr 16 2008

Keywords

  • 3-Phosphoglycerate kinase
  • Domain movement
  • Hinge
  • Site-directed mutagenesis
  • Small angle X-ray scattering

ASJC Scopus subject areas

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

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