Rossmann fold
The Rossmann fold is a protein structural motif found in proteins that bind nucleotides, especially the cofactor NAD. The structure with two repeats is composed of six parallel beta strands linked to two pairs of alpha helices in the topological order beta-alpha-beta-alpha-beta. Because each Rossmann fold can bind one nucleotide, binding domains for dinucleotides such as NAD consist of two paired Rossmann folds that each bind one nucleotide moiety of the cofactor molecule. Single Rossmann folds can bind mononucleotides such as the cofactor FMN.
The motif is named for Michael Rossmann, who first pointed out that this is a frequently occurring motif in nucleotide binding proteins, such as dehydrogenases.[1]
In 1989, Israel Hanukoglu from the Weizmann Institute of Science discovered that the consensus sequence for NADP binding site in some enzymes that utilize NADP differs from the NAD binding motif.[2] This discovery was used to re-engineer coenzyme specificities of enzymes.[3]
References
- ^ Rao S, Rossmann M (1973). "Comparison of super-secondary structures in proteins". J Mol Biol. 76 (2): 241–56. doi:10.1016/0022-2836(73)90388-4. PMID 4737475.
- ^ Hanukoglu, I.; Gutfinger, T. (1989). "cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases". Eur J Biochem. 180 (2): 479–84. doi:10.1111/j.1432-1033.1989.tb14671.x. PMID 2924777.
{{cite journal}}: Unknown parameter|month=ignored (help) - ^ Scrutton NS, Berry A, Perham RN (1990). "Redesign of the coenzyme specificity of a dehydrogenase by protein engineering". Nature. 343 (6253): 38–43. doi:10.1038/343038a0. PMID 2296288.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link)
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