Summary for 1BOS
| Entry DOI | 10.2210/pdb1bos/pdb |
| Descriptor | SHIGA-LIKE TOXIN I B SUBUNIT, alpha-D-galactopyranose-(1-4)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, alpha-D-galactopyranose-(1-4)-beta-D-galactopyranose, ... (5 entities in total) |
| Functional Keywords | toxin, receptor binding, protein-carbohydrate recognition, ob-fold |
| Biological source | Phage h30, Enterobacteria phage H-19B (,) |
| Total number of polymer chains | 20 |
| Total formula weight | 178077.60 |
| Authors | Ling, H.,Boodhoo, A.,Hazes, B.,Cummings, M.D.,Armstrong, G.D.,Brunton, J.L.,Read, R.J. (deposition date: 1998-01-13, release date: 1999-02-02, Last modification date: 2024-11-06) |
| Primary citation | Ling, H.,Boodhoo, A.,Hazes, B.,Cummings, M.D.,Armstrong, G.D.,Brunton, J.L.,Read, R.J. Structure of the shiga-like toxin I B-pentamer complexed with an analogue of its receptor Gb3. Biochemistry, 37:1777-1788, 1998 Cited by PubMed Abstract: Shiga-like toxin I (SLT-I) is a virulence factor of Escherichia coli strains that cause disease in humans. Like other members of the Shiga toxin family, it consists of an enzymatic (A) subunit and five copies of a binding subunit (the B-pentamer). The B-pentamer binds to a specific glycolipid, globotriaosylceramide (Gb3), on the surface of target cells and thereby plays a crucial role in the entry of the toxin. Here we present the crystal structure at 2.8 A resolution of the SLT-I B-pentamer complexed with an analogue of the Gb3 trisaccharide. The structure reveals a surprising density of binding sites, with three trisaccharide molecules bound to each B-subunit monomer of 69 residues. All 15 trisaccharides bind to one side of the B-pentamer, providing further evidence that this side faces the cell membrane. The structural model is consistent with data from site-directed mutagenesis and binding of carbohydrate analogues, and allows the rational design of therapeutic Gb3 analogues that block the attachment of toxin to cells. PubMed: 9485303DOI: 10.1021/bi971806n PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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