Conserved supersecondary structural motif in NAD-dependent dehydrogenases.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kutzenko AS,Lamzin VS,Popov VO

doi

10.1016/s0014-5793(98)00074-x

subject

Has Abstract

pub_date

1998-02-13 00:00:00

pages

105-9

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00074-X

journal_volume

423

pub_type

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