Acta NaturaeActa NaturaeActa Naturae2075-8251Acta Naturae Ltd1078410.32607/20758251-2009-1-3-89-93ArticlesСтатьиResearch ArticleAtomic Resolution Crystal Structure of NAD +Dependent Formate Dehydrogenase from Bacterium Moraxella sp. C-1Atomic Resolution Crystal Structure of NAD +Dependent Formate Dehydrogenase from Bacterium Moraxella sp. C-1ShabalinI GPolyakovK MTishkovV IPopovV Ovpopov@inbi.ras.ruA.N. Bach Institute of Biochemistry RASV.A. Engelhardt Institute of Molecular Biology RASA.N. Bach Institute of Biochemistry RAS1512200913NO3 (2009)№3 (2009)899317012020Copyright ©; 2009, Shabalin I.G., Polyakov K.M., Tishkov V.I., Popov V.O.Copyright ©; 2009, Shabalin I.G., Polyakov K.M., Tishkov V.I., Popov V.O.2009Shabalin I.G., Polyakov K.M., Tishkov V.I., Popov V.O.Shabalin I.G., Polyakov K.M., Tishkov V.I., Popov V.O.https://creativecommons.org/licenses/by/4.0https://actanaturae.ru/2075-8251/article/view/10784

The crystal structure of the ternary complex of NAD--dependent formate dehydrogenase from the methylotrophic bacterium Moraxella sp. С -1 with the cofactor (NAD-) and the inhibitor (azide ion) was established at 1.1 A resolution. The complex mimics the structure of the transition state of the enzymatic reaction. The structure was refined with anisotropic displacements parameters for non-hydrogen atoms to a R factor of 13.4%. Most of the nitrogen, oxygen, and carbon atoms were distinguished based on the analysis of the temperature factors and electron density peaks, with the result that side-chain rotamers of histidine residues and most of asparagine and glutamine residues were unambiguously determined. A comparative analysis of the structure of the ternary complex determined at the atomic resolution and the structure of this complex at 1.95 A resolution was performed. In the atomic resolution structure, the covalent bonds in the nicotinamide group are somewhat changed in agreement with the results of quantum mechanical calculations, providing evidence that the cofactor acquires a bipolar form in the transition state of the enzymatic reaction.

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