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The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion
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The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion
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Journal Article
The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion
2020
Overview
Protein secretion through type-three secretion systems (T3SS) is critical for motility and virulence of many bacteria. Proteins are transported through an export gate containing three proteins (FliPQR in flagella, SctRST in virulence systems). A fourth essential T3SS protein (FlhB/SctU) functions to “switch” secretion substrate specificity once the growing hook/needle reach their determined length. Here, we present the cryo-electron microscopy structure of an export gate containing the switch protein from a
Vibrio
flagellar system at 3.2 Å resolution. The structure reveals that FlhB/SctU extends the helical export gate with its four predicted transmembrane helices wrapped around FliPQR/SctRST. The unusual topology of the FlhB/SctU helices creates a loop wrapped around the bottom of the closed export gate. Structure-informed mutagenesis suggests that this loop is critical in gating secretion and we propose that a series of conformational changes in the T3SS trigger opening of the gate through interactions between FlhB/SctU and FliPQR/SctRST.
Export of proteins by type three secretion systems occurs through an export gate that is localized in the periplasm. Here, the authors present the cryo-EM structure of the
Vibrio mimicus
export gate complex with FlhB, which plays a major role in switching of the specificity of secretion substrates and propose a mechanism for export gate opening.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Bacterial Proteins - ultrastructure
/ Bacterial Secretion Systems - metabolism
/ Escherichia coli - metabolism
/ Exports
/ Flagella
/ Gating
/ Helices
/ Humanities and Social Sciences
/ Hydrophobic and Hydrophilic Interactions
/ Protein Structure, Secondary
/ Proteins
/ Science
/ Topology
