NAD-binding domains of dehydrogenases.

The nicotinamide adenine dinucleotide (NAD)-binding domains of dehydrogenases, containing a conserved double beta-alpha-beta-alpha-beta motif, are 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 alpha helix. Ferredoxin reductase seems to show convergent evolution, containing a single beta-alpha-beta motif that is similar both in its structure and in its interactions with the ligand to a region in dehydrogenases.

[1]  Michael G. Rossmann,et al.  Chemical and biological evolution of a nucleotide-binding protein , 1974, Nature.

[2]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.

[3]  M. Rossmann,et al.  Structure of Lactate Dehydrogenase at 2.8 Å Resolution , 1970, Nature.

[4]  C. Brändén,et al.  Relation between structure and function of α/β–protejns , 1980, Quarterly Reviews of Biophysics.

[5]  H. Sund Pyridine Nucleotide-Dependent Dehydrogenases , 1970, Springer Berlin Heidelberg.

[6]  N. Xuong,et al.  Crystal structure of rat liver dihydropteridine reductase. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[7]  K. Wilson,et al.  Crystal structure of NAD-dependent formate dehydrogenase. , 1992, European journal of biochemistry.

[8]  H. Muirhead,et al.  Design and synthesis of new enzymes based on the lactate dehydrogenase framework. , 1991, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[9]  R. Wierenga,et al.  INTERACTION OF PYROPHOSPHATE MOIETIES WITH ALPHA-HELIXES IN DINUCLEOTIDE BINDING-PROTEINS , 1985 .

[10]  P. Terpstra,et al.  Prediction of the Occurrence of the ADP-binding βαβ-fold in Proteins, Using an Amino Acid Sequence Fingerprint , 1986 .

[11]  P C Moody,et al.  Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 A resolution. , 1987, Journal of molecular biology.

[12]  A G Murzin,et al.  SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.

[13]  P. Karplus,et al.  Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family. , 1991, Science.

[14]  C. Branden,et al.  Introduction to protein structure , 1991 .

[15]  M. Hall,et al.  Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution. , 1993, Journal of molecular biology.

[16]  M Krook,et al.  Characteristics of short-chain alcohol dehydrogenases and related enzymes. , 1991, European journal of biochemistry.

[17]  S. Gover,et al.  Structure of 6-phosphogluconate dehydrogenase refined at 2 A resolution. , 1995, Acta crystallographica. Section D, Biological crystallography.

[18]  C. Brändén,et al.  X-Ray Studies of Horse Liver Alcohol Dehydrogenase , 1970 .

[19]  M G Rossmann,et al.  Comparison of super-secondary structures in proteins. , 1973, Journal of molecular biology.

[20]  Hans Eklund,et al.  Structure of Liver Alcohol Dehydrogenase at 2.9-Å Resolution , 1973 .

[21]  H. Eklund,et al.  Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase. , 1984, Biochemistry.