4G7X

Crystal structure of a complex between the CTXphi pIII N-terminal domain and the Vibrio cholerae TolA C-terminal domain

4G7X の概要

• エントリーDOI: 10.2210/pdb4g7x/pdb
• 関連するPDBエントリー: 4G7W
• 分子名称: Putative uncharacterized protein, TolA protein (3 entities in total)
• 機能のキーワード: membrane, protein binding-protein binding complex, protein binding/protein binding
• 由来する生物種: Vibrio cholerae; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26582.83

構造登録者

Kolappan, S.,Ford, C.G.,Craig, L. (登録日: 2012-07-20, 公開日: 2012-08-29, 最終更新日: 2024-10-09)

主引用文献

Ford, C.G.,Kolappan, S.,Phan, H.T.,Waldor, M.K.,Winther-Larsen, H.C.,Craig, L.
Crystal Structures of a CTX{varphi} pIII Domain Unbound and in Complex with a Vibrio cholerae TolA Domain Reveal Novel Interaction Interfaces.
J.Biol.Chem., 287:36258-36272, 2012

PubMed Abstract: Vibrio cholerae colonize the small intestine where they secrete cholera toxin, an ADP-ribosylating enzyme that is responsible for the voluminous diarrhea characteristic of cholera disease. The genes encoding cholera toxin are located on the genome of the filamentous bacteriophage, CTXϕ, that integrates as a prophage into the V. cholerae chromosome. CTXϕ infection of V. cholerae requires the toxin-coregulated pilus and the periplasmic protein TolA. This infection process parallels that of Escherichia coli infection by the Ff family of filamentous coliphage. Here we demonstrate a direct interaction between the N-terminal domain of the CTXϕ minor coat protein pIII (pIII-N1) and the C-terminal domain of TolA (TolA-C) and present x-ray crystal structures of pIII-N1 alone and in complex with TolA-C. The structures of CTXϕ pIII-N1 and V. cholerae TolA-C are similar to coliphage pIII-N1 and E. coli TolA-C, respectively, yet these proteins bind via a distinct interface that in E. coli TolA corresponds to a colicin binding site. Our data suggest that the TolA binding site on pIII-N1 of CTXϕ is accessible in the native pIII protein. This contrasts with the Ff family phage, where the TolA binding site on pIII is blocked and requires a pilus-induced unfolding event to become exposed. We propose that CTXϕ pIII accesses the periplasmic TolA through retraction of toxin-coregulated pilus, which brings the phage through the outer membrane pilus secretin channel. These data help to explain the process by which CTXϕ converts a harmless marine microbe into a deadly human pathogen.

PubMed: 22942280
DOI: 10.1074/jbc.M112.403386

実験手法

X-RAY DIFFRACTION (1.44 Å)