2XSC

Crystal structure of the cell-binding B oligomer of verotoxin-1 from E. coli

「1BOV」から置き換えられました

2XSC の概要

• エントリーDOI: 10.2210/pdb2xsc/pdb
• 関連するPDBエントリー: 1OJF
• 分子名称: SHIGA-LIKE TOXIN 1 SUBUNIT B, ZINC ION (3 entities in total)
• 機能のキーワード: toxin
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Secreted: P69178
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 38689.40

構造登録者

Stein, P.E.,Boodhoo, A.,Tyrrell, G.J.,Brunton, J.L.,Oeffner, R.D.,Bunkoczi, G.,Read, R.J. (登録日: 2010-09-27, 公開日: 2010-10-13, 最終更新日: 2024-11-13)

主引用文献

Stein, P.E.,Boodhoo, A.,Tyrrell, G.J.,Brunton, J.L.,Read, R.J.
Crystal Structure of the Cell-Binding B Oligomer of Verotoxin-1 from E. Coli.
Nature, 355:748-, 1992

PubMed Abstract: The Shiga toxin family, a group of cytotoxins associated with diarrhoeal diseases and the haemolytic uraemic syndrome, includes Shiga toxin from Shigella dysenteriae type 1 and verotoxins produced by enteropathogenic Escherichia coli. The family belongs to the A-B class of bacterial toxins, which includes the cholera toxin family, pertussis and diphtheria toxins. These toxins all have bipartite structures consisting of an enzymatic A subunit associated with a B oligomer which binds to specific cell-surface receptors, but their amino-acid sequences and pathogenic mechanisms differ. We have determined the crystal structure of the B oligomer of verotoxin-1 from E. coli. The structure unexpectedly resembles that of the B oligomer of the cholera toxin-like heat-labile enterotoxin from E. coli, despite the absence of detectable sequence similarity between these two proteins. This result implies a distant evolutionary relationship between the Shiga toxin and cholera toxin families. We suggest that the cell surface receptor-binding site lies in a cleft between adjacent subunits of the B pentamer, providing a potential target for drugs and vaccines to prevent toxin binding and effect.

PubMed: 1741063
DOI: 10.1038/355748A0

実験手法

X-RAY DIFFRACTION (2.052 Å)