1DM0

SHIGA TOXIN

Summary for 1DM0

• Entry DOI: 10.2210/pdb1dm0/pdb
• Descriptor: SHIGA TOXIN A SUBUNIT, SHIGA TOXIN B SUBUNIT (3 entities in total)
• Functional Keywords: ab5 structure, polypeptide a, blocking, active site, toxin
• Biological source: Shigella dysenteriae; More
• Total number of polymer chains: 12
• Total formula weight: 140109.61

Authors

Fraser, M.E.,Chernaia, M.M.,Kozlov, Y.V.,James, M.N. (deposition date: 1999-12-13, release date: 1999-12-30, Last modification date: 2024-10-16)

Primary citation

Fraser, M.E.,Chernaia, M.M.,Kozlov, Y.V.,James, M.N.
Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution.
Nat.Struct.Biol., 1:59-64, 1994

PubMed Abstract: 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.

PubMed: 7656009
DOI: 10.1038/nsb0194-59

Experimental method

X-RAY DIFFRACTION (2.5 Å)