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

FEBS Letters
Andrea VargaMária Vas

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 beta-strand L, under the concerted action of both substrates.

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Citations

Jul 23, 2013·Journal of Bioenergetics and Biomembranes·Alonso A López-ZavalaRogerio R Sotelo-Mundo
Feb 26, 2011·The Journal of Biological Chemistry·Louiza ZerradMatthew W Bowler
Jun 4, 2011·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Amlan RoychowdhuryAmit Kumar Das
Jan 28, 2014·PLoS Computational Biology·Zoltan PalmaiErika Balog
Jun 7, 2012·The Journal of Chemical Physics·Jeremy SchofieldRaymond Kapral
Dec 4, 2012·European Journal of Pharmaceutical Sciences : Official Journal of the European Federation for Pharmaceutical Sciences·Andrea VargaMária Vas
Dec 1, 2009·Journal of Molecular Biology·James P MarstonJonathan P Waltho
Dec 22, 2007·Biochemical and Biophysical Research Communications·Andrea VargaMária Vas
Apr 8, 2015·Nature Methods·Daniel FrankeDmitri I Svergun
Apr 20, 2010·Journal of the American Chemical Society·Matthew J CliffJonathan P Waltho
Dec 12, 2021·Proceedings of the National Academy of Sciences of the United States of America·Hiromasa YagiTakanori Kigawa

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