1etn
From Proteopedia
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MOLECULAR STRUCTURE OF THE TOXIC DOMAIN OF HEAT-STABLE ENTEROTOXIN PRODUCED BY A PATHOGENIC STRAIN OF ESCHERICHIA COLI
Overview
Heat-stable enterotoxins are a family of toxin peptides that are produced, by enterotoxigenic Escherichia coli and consist of 18 and 19 amino acid, residues (Aimoto, S., Takao, T., Shimonishi, Y., Hara, S., Takeda, T., Takeda, Y., and Miwatani, T. (1982) Eur. J. Biochem. 129, 257-263). A, synthetic fully toxic analog of the enterotoxin, Mpr5-STp(5-17), where Mpr, is beta-mercaptopropionic acid and which consists of 13 amino acid, residues from Cys5 to Cys17 in a heat-stable enterotoxin but is deaminated, at its N terminus (Kubota, H., Hidaka, Y., Ozaki, H., Ito, H., Hirayama, T., Takeda, Y., and Shimonishi, Y. (1989) Biochem. Biophys. Res. Commun., 161, 229-235), has been crystalized from water, and its crystal structure, has been solved by a direct method and refined by least square procedures, to give an R factor of 0.089. The crystal belongs to the orthorhombic, space group P2(1)2(1)2(1) with unit cell constants a = 21.010 (2) A, b =, 27.621 (4) A, and c = 12.781 (1) A. The asymmetric unit of the crystals, contains one peptide molecule with 13 water molecules. A right-hand spiral, peptide backbone extends throughout the molecule. Three beta-turns are, located along this spiral and fixed tightly by three intramolecular, disulfide linkages. The actual structure predicts the biniding region on, the enterotoxin to the receptor protein on the membrane of rat intestinal, epithelial cells.
About this Structure
1ETN is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Molecular structure of the toxin domain of heat-stable enterotoxin produced by a pathogenic strain of Escherichia coli. A putative binding site for a binding protein on rat intestinal epithelial cell membranes., Ozaki H, Sato T, Kubota H, Hata Y, Katsube Y, Shimonishi Y, J Biol Chem. 1991 Mar 25;266(9):5934-41. PMID:2005130 [[Category: ]]
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