2F1N

Structure of CdtB, the biologically active subunit of Cytolethal Distending Toxin

2F1N の概要

• エントリーDOI: 10.2210/pdb2f1n/pdb
• 分子名称: Cytolethal distending toxin subunit B (2 entities in total)
• 機能のキーワード: cytolethal distending toxin, cdt, e.coli, toxin, dnase i, microbatch
• 由来する生物種: Escherichia coli
• 細胞内の位置: Secreted : Q46669
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28768.29

構造登録者

Hontz, J.S.,Yoder, M.D.,Dreyfus, L.A. (登録日: 2005-11-14, 公開日: 2006-07-04, 最終更新日: 2023-08-23)

主引用文献

Hontz, J.S.,Villar-Lecumberri, M.T.,Potter, B.M.,Yoder, M.D.,Dreyfus, L.A.,Laity, J.H.
Differences in Crystal and Solution Structures of the Cytolethal Distending Toxin B Subunit: RELEVANCE TO NUCLEAR TRANSLOCATION AND FUNCTIONAL ACTIVATION.
J.Biol.Chem., 281:25365-25372, 2006

PubMed Abstract: Cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis in eukaryotic cells, which are mediated by the DNA-damaging CdtB subunit. Here we report the first x-ray structure of an isolated CdtB subunit (Escherichia coli-II CdtB, EcCdtB). In conjunction with previous structural and biochemical observations, active site structural comparisons between free and holotoxin-assembled CdtBs suggested that CDT intoxication is contingent upon holotoxin disassembly. Solution NMR structural and 15N relaxation studies of free EcCdtB revealed disorder in the interface with the CdtA and CdtC subunits (residues Gly233-Asp242). Residues Leu186-Thr209 of EcCdtB, which encompasses tandem arginine residues essential for nuclear translocation and intoxication, were also disordered in solution. In stark contrast, nearly identical well defined alpha-helix and beta-strand secondary structures were observed in this region of the free and holotoxin CdtB crystallographic models, suggesting that distinct changes in structural ordering characterize subunit disassembly and nuclear localization factor binding functions.

PubMed: 16809347
DOI: 10.1074/jbc.M603727200

実験手法

X-RAY DIFFRACTION (1.73 Å)