5EKQ

The structure of the BamACDE subcomplex from E. coli

Summary for 5EKQ

• Entry DOI: 10.2210/pdb5ekq/pdb
• Descriptor: Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamD, Outer membrane protein assembly factor BamC, ... (4 entities in total)
• Functional Keywords: membrane protein, insertase, beta-barrel, outer membrane protein
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 4
• Total formula weight: 159124.36

Authors

Bakelar, J.,Buchanan, S.K.,Noinaj, N. (deposition date: 2015-11-04, release date: 2016-01-20, Last modification date: 2024-10-30)

Primary citation

Bakelar, J.,Buchanan, S.K.,Noinaj, N.
The structure of the beta-barrel assembly machinery complex.
Science, 351:180-186, 2016

PubMed Abstract: β-Barrel outer membrane proteins (OMPs) are found in the outer membranes of Gram-negative bacteria and are essential for nutrient import, signaling, and adhesion. A 200-kilodalton five-component complex called the β-barrel assembly machinery (BAM) complex has been implicated in the biogenesis of OMPs. We report the structure of the BAM complex from Escherichia coli, revealing that binding of BamCDE modulates the conformation of BamA, the central component, which may serve to regulate the BAM complex. The periplasmic domain of BamA was in a closed state that prevents access to the barrel lumen, which indicates substrate OMPs may not be threaded through the barrel during biogenesis. Further, conformational shifts in the barrel domain lead to opening of the exit pore and rearrangement at the lateral gate.

PubMed: 26744406
DOI: 10.1126/science.aad3460

Experimental method

X-RAY DIFFRACTION (3.392 Å)