β-barrel

Ribbon model of a sucrose- specific porin from Salmonella : side view (parallel to the membrane) of the β-barrel structure with the antiparallel β-sheets.

A β-barrel (engl. Β-barrel ) is a protein structural motif, particularly in the pore-forming proteins occurs. It consists of at least five β-sheets that are arranged in a circle and thus form a tube (the pore ), which is mostly responsible for the protein's function as a transport protein . The inside diameter of such a pore can be from a few to several dozen angstroms .

See also

• OB folding

literature

• AG Murzin, AM Lesk, C. Chothia: Principles determining the structure of beta-sheet barrels in proteins. II. The observed structures. In: Journal of Molecular Biology . Volume 236, Number 5, March 1994, pp. 1382-1400. PMID 8126727 .
• WM Liu: Shear numbers of protein beta-barrels: definition refinements and statistics. In: Journal of molecular biology . Volume 275, Number 4, January 1998, pp. 541-545. doi: 10.1006 / jmbi.1997.1501 . PMID 9466929 . (Review).
• WC Wimley: The versatile beta-barrel membrane protein. In: Current opinion in structural biology. Volume 13, Number 4, August 2003, pp. 404-411, ISSN  0959-440X . PMID 12948769 . (Review).

Individual evidence

1. ↑ Forst, D. et al. (1998): Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. In: Nat. Struct. Biol. Vol. 5, pp. 37-46. PMID 9437428 PDB  1A0S

Web links

• Images and examples of transmembrane beta-barrels
• Stockholm Bioinformatics Center review of transmembrane proteins
• The Lipocalin Website ( Memento of February 26, 2008 in the Internet Archive )