Rossmann fold

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An example of the Rossmann fold, a structural domain of a decarboxylase protein from the bacterium Staphylococcus epidermidis (PDB ID 1G5Q) with the bound flavin mononucleotide cofactor shown.

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]


  1. ^ 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. 
  2. ^ 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. 
  3. ^ 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.