Reference : Stability domains, substrate-induced conformational changes, and hinge-bending motions i...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/15405
Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study
English
Zecchinon, Laurent mailto [Université de Liège - ULg > Département de morphologie et pathologie > Pathologie spéciale et autopsies >]
Oriol, A. [> > > >]
Netzel, U. [> > > >]
Svennberg, J. [> > > >]
Gerardin-Otthiers, N. [> > > >]
Feller, Georges mailto [Université de Liège - ULg > Département des sciences de la vie > Labo de biochimie >]
16-Dec-2005
Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc
280
50
41307-41314
Yes (verified by ORBi)
International
0021-9258
Bethesda
[en] The cold-active phosphoglycerate kinase from the Antarctic bacterium Pseudomonas sp. TACII18 exhibits two distinct stability domains in the free, open conformation. It is shown that these stability domains do not match the structural N- and C-domains as the heat-stable domain corresponds to about 80 residues of the C-domain, including the nucleotide binding site, whereas the remaining of the protein contributes to the main heat-labile domain. This was demonstrated by spectroscopic and microcalorimetric analyses of the native enzyme, of its mutants, and of the isolated recombinant structural domains. It is proposed that the heat-stable domain provides a compact structure improving the binding affinity of the nucleotide, therefore increasing the catalytic efficiency at low temperatures. Upon substrate binding, the enzyme adopts a uniformly more stable closed conformation. Substrate-induced stability changes suggest that the free energy of ligand binding is converted into an increased conformational stability used to drive the hinge-bending motions and domain closure.
http://hdl.handle.net/2268/15405
10.1074/jbc.M506464200

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