Structure of the Core of the Type Three Secretion System Export Apparatus

Autor: Lucas Kuhlen, Justin C. Deme, Susan M. Lea, Samuel Wagner, Mehari Tesfazgi Mebrhatu, Boris Macek, Steven Johnson, Tariq Ganief, Patrizia Abrusci, Tobias Dietsche, Joseph J. E. Caesar, Carol V. Robinson, Joseph Gault
Jazyk: angličtina
Rok vydání: 2018
Předmět:
Zdroj: Nature structural & molecular biology
DOI: 10.1101/249128
Popis: SummaryExport of proteins through type three secretion systems is critical for bacterial motility and virulence of many major bacterial pathogens. Three putative integral membrane proteins (FliP/FliQ/FliR) are suggested to form the core of an export gate in the inner membrane, but their structure, assembly and location within the final nanomachine remain unclear. We here present the structure of this complex at 4.2 Å by cryo-electron microscopy. None of the subunits adopt canonical integral membrane protein topologies and common helix-turn-helix structural elements allow them to form a helical assembly with 5:4:1 stoichiometry. Fitting of the structure into reconstructions of intact secretion systems localize the export gate as a core component of the periplasmic portion of the machinery, and cross-linking experiments confirm this observation. This study thereby identifies the export gate as a key element of the secretion channel and implies that it primes the helical architecture of the components assembling downstream.One Sentence SummaryThe core of the T3SS export gate forms a supra-membrane helical assembly
Databáze: OpenAIRE