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TitleDarobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells.
Journal, issue, pagesAngew Chem Int Ed Engl, Vol. 62, Issue 34, Page e202218783, Year 2023
Publish dateAug 21, 2023
AuthorsSamuel F Haysom / Jonathan Machin / James M Whitehouse / Jim E Horne / Katherine Fenn / Yue Ma / Hassane El Mkami / Nils Böhringer / Till F Schäberle / Neil A Ranson / Sheena E Radford / Christos Pliotas /
PubMed AbstractThe β-barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram-negative bacteria, and represents a promising antimicrobial target. Several conformational ...The β-barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram-negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but all have been obtained under conditions which lack the unique features and complexity of the outer membrane (OM). Here, we use Pulsed Electron-Electron Double Resonance (PELDOR, or DEER) spectroscopy distance measurements to interrogate the conformational ensemble of the BAM complex in E. coli cells. We show that BAM adopts a broad ensemble of conformations in the OM, while in the presence of the antibiotic darobactin B (DAR-B), BAM's conformational equilibrium shifts to a restricted ensemble consistent with the lateral closed state. Our in-cell PELDOR findings are supported by new cryoEM structures of BAM in the presence and absence of DAR-B. This work demonstrates the utility of PELDOR to map conformational changes in BAM within its native cellular environment.
External linksAngew Chem Int Ed Engl / PubMed:37162386 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.5 Å
Structure data

16268

8bvq

EMDB-16268, PDB-8bvq:
E. coli BAM complex (BamABCDE) bound to darobactin B
Method: EM (single particle) / Resolution: 3.3 Å

16282

8bwc

EMDB-16282, PDB-8bwc:
E. coli BAM complex (BamABCDE) wild-type
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • escherichia coli (E. coli)
  • photorhabdus heterorhabditis (bacteria)
  • escherichia coli bl21(de3) (bacteria)
KeywordsMEMBRANE PROTEIN / Outer Membrane Protein / Protein Folding / Antibiotic / beta barrel

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