OB folding

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Representation of a β-sheet. The atoms of the amino acids involved and the hydrogen bonds are shown as opaque.
S1 domain of exosome components 3 , part of the human exosome complex . The OB fold is on the left in the illustration.

The OB- fold refers to a type of protein folding (protein structure). The acronym is derived from O ligonucleotide / Oligosaccharide B inding.

This steric protein structure is found, for example, in cell walls and is used for molecule-specific interaction, in a broader sense for metabolism and information exchange between living cells.

The OB-fold consists of five β-sheets , which are arranged in a circle and thus form a barrel-shaped tertiary structure , a so-called beta-barrel . OB folds have been found in various proteins such as B. Nucleases and synthetases detected and are characterized by a low sequence homology , but a high structural homology . This means that the amino acid sequences of various OB folds can differ greatly from one another, but they still have a similar spatial structure.

Individual evidence

  1. ^ V. Agrawal, KV Kishan: OB-fold: Growing bigger with functional consistency. In: Curr Protein Pept Sci. 4 (3), Jun 2003, pp. 195-206.
  2. Biocompare: Cytosolic Expression Of Green Fluorescent Protein (GFP) And Its Derivatives In The Yeast Saccharomyces Cerevisiae: Detection In Vivo Using The Varian Cary Eclipse.
  3. Petra Averhoff: Characterization of the specificity of human neutrophil elastase for Shigella flexneri virulence factors. Dissertation . University of Berlin.
  4. AG Murzin et al .: OB (oligonucleotide / oligosaccharide binding) -fold: common structural and functional solution for non-homologous sequences. In: EMBO J. Band 12 , no. 3 , March 1993, p. 861-867 , PMC 413284 (free full text).
  5. ^ DL Theobald, RM Mitton-Fry, DS Wuttke: Nucleic acid recognition by OB-fold proteins. In: Annu Rev Biophys Biomol Struct. tape 32 , February 2003, p. 115-133 , doi : 10.1146 / annurev.biophys.32.110601.142506 .