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PDBsum entry 1dm0
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Contents |
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264 a.a.
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(+ 4 more)
69 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the holotoxin from shigella dysenteriae at 2.5 a resolution.
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Authors
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M.E.Fraser,
M.M.Chernaia,
Y.V.Kozlov,
M.N.James.
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Ref.
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Nat Struct Biol, 1994,
1,
59-64.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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X-Ray crystal structure of the shiga toxin
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Authors
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M.E.Fraser,
M.M.Chernaia,
Y.V.Kozlov,
M.N.James.
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Ref.
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protein toxin structure, ...
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Secondary reference #2
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Title
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Purification and crystallization of shiga toxin from shigella dysenteriae.
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Authors
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Y.V.Kozlov,
M.M.Chernaia,
M.E.Fraser,
M.N.James.
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Ref.
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J Mol Biol, 1993,
232,
704-706.
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PubMed id
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