1BOS の概要
| エントリーDOI | 10.2210/pdb1bos/pdb |
| 分子名称 | 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) |
| 機能のキーワード | toxin, receptor binding, protein-carbohydrate recognition, ob-fold |
| 由来する生物種 | Phage h30, Enterobacteria phage H-19B (,) |
| タンパク質・核酸の鎖数 | 20 |
| 化学式量合計 | 178077.60 |
| 構造登録者 | Ling, H.,Boodhoo, A.,Hazes, B.,Cummings, M.D.,Armstrong, G.D.,Brunton, J.L.,Read, R.J. (登録日: 1998-01-13, 公開日: 1999-02-02, 最終更新日: 2024-11-06) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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