title: [Symmetry-regulated dynamics of multi-enzyme complexes. A model of a pyruvate dehydrogenase complex from Escherichia coli].
abstract: A dynamic model for quaternary structure of a multienzyme complex is considered. The model is based on the supposition of simultaneously existing similar subunits in a number of different conformational states in the "core" of the multienzyme complex. It is supposed that cyclic conformational transitions of the "core" subunits conserve the symmetry of the entire complex. Such transitions drive the core dynamics as well as the suprastructural multienzyme dynamics. The dynamic model is constructed for the pyruvate dehydrogenase complex from E. coli in a supposition of three different conformers existing in its "core" which correspond to the three steps of the cyclic catalytic process. The model is in accordance with the data from the literature.
authors.forename: B N
authors.initials: BN
authors.lastname: Gol'dshteĭn
authors.forename: V V
authors.initials: VV
authors.lastname: Kornilov
mesh_terms: D000107:Acetylation; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011768:Pyruvate Dehydrogenase Complex / Q000032:analysis*
chemical_list: D046911:Macromolecular Substances; D011768:Pyruvate Dehydrogenase Complex
vernacular_title: Upravliaemaia simmetrieĭ dinamika mul'tifermentnykh kompleksov. Model' piruvatdegidrogenaznogo kompleksa iz Escherichia coli.