Rossmann fold
The Rossmann fold is a protein structural motif found in proteins that bind nucleotides, such as enzyme cofactors FAD, NAD+, and NADP+.[1] The structure is composed of up to seven mostly parallel beta strands. The first two strands are connected by an α- helix. The structures of segments between additional strands vary greatly and may include structures such as short helical segments and coils.[1]
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.[2]
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.[3] This discovery was used to re-engineer coenzyme specificities of enzymes.[4]
References
- 1 2 Hanukoglu I (2015). "Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide binding sites". Biochem Mol Biol Educ. 43 (3): 206–209. doi:10.1002/bmb.20849. PMID 25704928.
- ↑ Rao ST, Rossmann MG (May 1973). "Comparison of super-secondary structures in proteins". Journal of Molecular Biology. 76 (2): 241–56. doi:10.1016/0022-2836(73)90388-4. PMID 4737475.
- ↑ Hanukoglu I, Gutfinger T (Mar 1989). "cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases". European Journal of Biochemistry / FEBS. 180 (2): 479–84. doi:10.1111/j.1432-1033.1989.tb14671.x. PMID 2924777.
- ↑ Scrutton NS, Berry A, Perham RN (Jan 1990). "Redesign of the coenzyme specificity of a dehydrogenase by protein engineering". Nature. 343 (6253): 38–43. doi:10.1038/343038a0. PMID 2296288.