title: Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase.
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.
authors.affiliation: Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H-1518 Budapest, P.O. Box 7, Hungary.
authors.forename: Andrea
authors.initials: A
authors.lastname: Varga
authors.forename: Beáta
authors.initials: B
authors.lastname: Flachner
authors.forename: Peter
authors.initials: P
authors.lastname: Konarev
authors.forename: Eva
authors.initials: E
authors.lastname: Gráczer
authors.forename: Judit
authors.initials: J
authors.lastname: Szabó
authors.forename: Dmitri
authors.initials: D
authors.lastname: Svergun
authors.forename: Péter
authors.initials: P
authors.lastname: Závodszky
authors.forename: Mária
authors.initials: M
authors.lastname: Vas
mesh_terms: D005988:Glyceric Acids / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010735:Phosphoglycerate Kinase / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D005988:Glyceric Acids; C005156:3-phosphoglycerate; D010735:Phosphoglycerate Kinase