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 Cited by 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: 7656009DOI: 10.1038/nsb0194-59 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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