1dm0
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(New page: 200px<br /><applet load="1dm0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dm0, resolution 2.5Å" /> '''SHIGA TOXIN'''<br /> ...)
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Revision as of 01:11, 25 November 2007
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SHIGA TOXIN
Overview
Shigella dysenteriae is the pathogen responsible for the severe form of, dysentery in humans. It produces Shiga toxin, the prototype of a family of, closely related bacterial protein toxins. We have determined the structure, of the holotoxin, an AB5 hexamer, by X-ray crystallography. The five B, subunits form a pentameric ring, encircling a helix at the carboxy, terminus of the A subunit. The A subunit interacts with the B pentamer via, this C-terminal helix and a four-stranded mixed beta-sheet. The fold of, the rest of the A subunit is similar to that of the A chain of the plant, toxin ricin; both are N-glycosidases. However, the active site in the, bacterial holotoxin is blocked by a segment of polypeptide chain. These, residues of the A subunit would be released as part of the activation, mechanism of the toxin.
About this Structure
1DM0 is a Protein complex structure of sequences from Shigella dysenteriae. Active as rRNA N-glycosylase, with EC number 3.2.2.22 Full crystallographic information is available from OCA.
Reference
Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution., Fraser ME, Chernaia MM, Kozlov YV, James MN, Nat Struct Biol. 1994 Jan;1(1):59-64. PMID:7656009
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