Conserved supersecondary structural motif in NAD-dependent dehydrogenases.
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 beta-sheet with one complete and one partial Rossmann fold units and two alpha-helices, the long helix, adjacent to and running roughly parallel with the beta-sheet plane and the helix connecting two Rossmann folds.
Kutzenko
A S
AS
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
Lamzin
V S
VS
Popov
V O
VO
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D009243:NAD / Q000378:metabolism*; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary
D009243:NAD; D010088:Oxidoreductases