Large-Scale Conformational Changes of FhaC Provide Insights Into the Two-Partner Secretion Mechanism.

ABSTRACT: The Two-Partner secretion pathway mediates protein transport across the outer membrane of Gram-negative bacteria. TpsB transporters belong to the Omp85 superfamily, whose members catalyze protein insertion into, or translocation across membranes without external energy sources. They are composed of a transmembrane β barrel preceded by two periplasmic POTRA domains that bind the incoming protein substrate. Here we used an integrative approach combining in vivo assays, mass spectrometry, nuclear magnetic resonance and electron paramagnetic resonance techniques suitable to detect minor states in heterogeneous populations, to explore transient conformers of the TpsB transporter FhaC. This revealed substantial, spontaneous conformational changes on a slow time scale, with parts of the PO

SUBMITTER: Sicoli G 

PROVIDER: S-EPMC9355242 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature