Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles and Escherichia coli.

ABSTRACT: The β-barrel assembly machinery (BAM) mediates the folding and insertion of the majority of outer membrane proteins (OMPs) in gram-negative bacteria. BAM is a penta-heterooligomeric complex consisting of the central β-barrel BamA and four interacting lipoproteins BamB, C, D, and E. The conformational switching of BamA between inward-open (IO) and lateral-open (LO) conformations is required for substrate recognition and folding. However, the mechanism for the lateral gating or how the structural details observed in vitro correspond with the cellular environment remains elusive. In this study, we addressed these questions by characterizing the conformational heterogeneity of BamAB, BamACDE, and BamABCDE complexes in detergent micelles and/or Escherichia coli using pulsed dipolar elect

SUBMITTER: Gopinath A 

PROVIDER: S-EPMC10833450 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature