Rossmann folding

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An example of a Rossmann fold. A structural element of a decarboxylase of the bacterium Staphylococcus epidermidis with the bound cofactor flavin mononucleotide ( PDB  1G5Q ).

The Rossmann fold is a functional super- secondary structure or a motif in proteins in which two units of the form beta-alpha-beta-alpha-beta - i.e., β-sheets connected via α-helices - combine to form dinucleotides such as nicotinamide adenine dinucleotide ( NAD + ) to bind.

The Rossmann convolution is one of the first frequently identified structural domains. It was named after its discoverer Michael Rossmann and probably represents an original dinucleotide binding domain . a. in the three dehydrogenases of glycolysis .

literature

  • Donald Voet, Judith G. Voet, Charlotte W. Pratt: Textbook of Biochemistry . Translation edited by Annette G. Beck-Sickinger and Ulrich Hahn. Wiley-VCH Verlag , 2002
  • JM Berg, JL Tymoczko, L. Stryer: Biochemistry . Translated from English by B. Häcker, A. Held, B. Jarosch, C. Lange, K. Mahlke, G. Maxam, L. Seidel, N. Zellerhoff. 6th edition, Spectrum, 2007

Individual evidence

  1. ↑ Hanukoglu I: Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide binding sites . In: Biochem Mol Biol Educ . 43, No. 3, 2015, pp. 206-209. doi : 10.1002 / bmb.20849 . PMID 25704928 .
  2. ↑ Michael G. Rossmann , Dino Moras & Kenneth W. Olsen: Chemical and biological evolution of a nucleotide-binding protein . In: Nature . 250, No. 5463, July 1974, pp. 194-99.