1SR4

Crystal Structure of the Haemophilus ducreyi cytolethal distending toxin

1SR4 の概要

• エントリーDOI: 10.2210/pdb1sr4/pdb
• 分子名称: Cytolethal distending toxin subunit A, cytolethal distending toxin protein B, cytolethal distending toxin protein C, ... (5 entities in total)
• 機能のキーワード: toxin, bacterial, haemophilus ducreyi, virulence, dna damage, genotoxin, cytotoxins, cell cycle, apoptosis, lectin, deoxyribonuclease i
• 由来する生物種: Haemophilus ducreyi; 詳細
• 細胞内の位置: Cell outer membrane; Lipid-anchor (Probable): O06522
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 72320.42

構造登録者

Nesic, D.,Hsu, Y.,Stebbins, C.E. (登録日: 2004-03-22, 公開日: 2004-06-15, 最終更新日: 2024-11-06)

主引用文献

Nesic, D.,Hsu, Y.,Stebbins, C.E.
Assembly and Function of a Bacterial Genotoxin
Nature, 429:429-433, 2004

PubMed Abstract: The tripartite cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis in eukaryotic cells. The subunits CdtA and CdtC associate with the nuclease CdtB to form a holotoxin that translocates CdtB into the host cell, where it acts as a genotoxin by creating DNA lesions. Here we show that the crystal structure of the holotoxin from Haemophilus ducreyi reveals that CDT consists of an enzyme of the DNase-I family, bound to two ricin-like lectin domains. CdtA, CdtB and CdtC form a ternary complex with three interdependent molecular interfaces, characterized by globular, as well as extensive non-globular, interactions. The lectin subunits form a deeply grooved, highly aromatic surface that we show to be critical for toxicity. The holotoxin possesses a steric block of the CdtB active site by means of a non-globular extension of the CdtC subunit, and we identify putative DNA binding residues in CdtB that are essential for toxin activity.

PubMed: 15164065
DOI: 10.1038/nature02532

実験手法

X-RAY DIFFRACTION (2 Å)