NAD-binding domains of dehydrogenases

NAD-binding domains of dehydrogenases The nicotinamide adenine dinucleotide (NAD)-binding domains of dehydrogenases, containing a conserved double β-α-β-α-β motif, are a common structural feature of many enzymes that bind NAD, nicotinamide adenine dinucleotide phosphate (NADP) and related cofactors. Features of this folding pattern that create a natural binding site for such molecules have been described. The domain continues to appear in many structures, in the form of a common core with different peripheral additions or variations. Other structures that bind NAD and related molecules use entirely different topologies, although, in many, a phosphate group appears at the N terminus of an α helix. Ferredoxin reductase seems to show convergent evolution, containing a single β-α-β motif that is similar both in its structure and in its interactions with the ligand to a region in dehydrogenases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Structural Biology Elsevier

NAD-binding domains of dehydrogenases

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Publisher
Elsevier
Copyright
Copyright © 1995 Elsevier Ltd
ISSN
0959-440x
D.O.I.
10.1016/0959-440X(95)80010-7
Publisher site
See Article on Publisher Site

Abstract

The nicotinamide adenine dinucleotide (NAD)-binding domains of dehydrogenases, containing a conserved double β-α-β-α-β motif, are a common structural feature of many enzymes that bind NAD, nicotinamide adenine dinucleotide phosphate (NADP) and related cofactors. Features of this folding pattern that create a natural binding site for such molecules have been described. The domain continues to appear in many structures, in the form of a common core with different peripheral additions or variations. Other structures that bind NAD and related molecules use entirely different topologies, although, in many, a phosphate group appears at the N terminus of an α helix. Ferredoxin reductase seems to show convergent evolution, containing a single β-α-β motif that is similar both in its structure and in its interactions with the ligand to a region in dehydrogenases.

Journal

Current Opinion in Structural BiologyElsevier

Published: Dec 1, 1995

References

  • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    Brenner, SE; Chothia, C; Hubbard, TJP; Murzin, AG
  • Crystal structure of rat liver dihydropteridine reductase
    Varughese, KI; Skinner, MM; Whiteley, JM; Matthews, DA; Xuong, NH

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