Conserved supersecondary structural motif in NAD‐dependent dehydrogenases

FEBS Letters

Kutzenko, Alexey S³  Popov, Vladimir O¹  Lamzin, Victor S² 

[1] Laboratory of Enzyme Engineering, A.N. Bakh Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr., 33, 117071 Moscow, Russia;EMBL Outstation, DESY, Notkestraße 85, 22603 Hamburg, Germany;Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, 117984 Moscow, Russia

关键词: Nicotinamide adenine dinucleotide-dependent dehydrogenase;    d-specific Dehydrogenase;    Conserved structural motif;    Rossmann fold domain;    ADH;    alcohol dehydrogenase;    DHFR;    dihydrofolate reductase;    FD;    flavodoxin;    FDH;    formate dehydrogenase;    DGDH;    d-glycerate dehydrogenase;    GRS;    glutathione reductase;    GPDH;    glyceraldehyde-3-phosphate dehydrogenase;    LDH;    lactate dehydrogenase;    DLDH;    d-lactate dehydrogenase;    MDH;    malate dehydrogenase;    PGDH;    d-phosphoglycerate dehydrogenase;   

DOI  :  10.1016/S0014-5793(98)00074-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

l- and d-specific nicotinamide adenine dinucleotide (NAD)-dependent dehydrogenases map to the same structural protein superfamily as defined by the Structural Classification of Proteins (SCOP) and are based on the Rossmann fold type domains. A detailed classification of these domains is proposed using a novel diagnostic parameter of the rms per aligned pair. The catalytic domain in d-specific dehydrogenases shows a strong structural homology to the coenzyme binding domain. A topologically conserved part within the dehydrogenase superfamily reveals a supersecondary structural motif comprising the 5-stranded left-handedly twisted parallel β-sheet with one complete and one partial Rossmann fold units and two α-helices, the long helix, adjacent to and running roughly parallel with the β-sheet plane and the helix connecting two Rossmann folds.

【 授权许可】

Unknown