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Conserved supersecondary structural motif in NAD‐dependent dehydrogenases
Author(s) -
Kutzenko Alexey S,
Lamzin Victor S,
Popov Vladimir O
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00074-x
Subject(s) - nad+ kinase , nicotinamide adenine dinucleotide , structural motif , superfamily , cofactor , dehydrogenase , crystallography , protein structure , homology (biology) , biology , stereochemistry , biochemistry , chemistry , enzyme , amino acid , gene
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.