1dm0
From Proteopedia
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[[Image:1dm0.gif|left|200px]] | [[Image:1dm0.gif|left|200px]] | ||
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'''SHIGA TOXIN''' | '''SHIGA TOXIN''' | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Shigella dysenteriae]] | [[Category: Shigella dysenteriae]] | ||
| - | [[Category: | + | [[Category: RRNA N-glycosylase]] |
[[Category: Chernaia, M M.]] | [[Category: Chernaia, M M.]] | ||
[[Category: Fraser, M E.]] | [[Category: Fraser, M E.]] | ||
[[Category: James, M N.]] | [[Category: James, M N.]] | ||
[[Category: Kozlov, Y V.]] | [[Category: Kozlov, Y V.]] | ||
| - | [[Category: | + | [[Category: Ab5 structure]] |
| - | [[Category: | + | [[Category: Active site]] |
| - | [[Category: | + | [[Category: Blocking]] |
| - | [[Category: | + | [[Category: Polypeptide some]] |
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Revision as of 11:00, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 14:00:12 2008
