5D0Q

BamACDE complex, outer membrane beta-barrel assembly machinery (BAM) complex

Summary for 5D0Q

• Entry DOI: 10.2210/pdb5d0q/pdb
• Related: 5D0O
• Descriptor: Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamC, Outer membrane protein assembly factor BamD, ... (4 entities in total)
• Functional Keywords: outer membrane biogenesis, outer membrane beta-barrel assembly machinery complex, e.coli, outer membrane insertion., protein transport
• Biological source: Escherichia coli K-12; More
• Cellular location: Cell outer membrane : P0A940; Cell outer membrane ; Lipid-anchor : P0A903 P0AC02 P0A937
• Total number of polymer chains: 8
• Total formula weight: 341378.61

Authors

Gu, Y.,Paterson, N.,Zeng, Y.,Dong, H.,Wang, W.,Dong, C. (deposition date: 2015-08-03, release date: 2016-03-09)

Primary citation

Gu, Y.,Li, H.,Dong, H.,Zeng, Y.,Zhang, Z.,Paterson, N.G.,Stansfeld, P.J.,Wang, Z.,Zhang, Y.,Wang, W.,Dong, C.
Structural basis of outer membrane protein insertion by the BAM complex.
Nature, 531:47-52, 2016

PubMed Abstract: All Gram-negative bacteria, mitochondria and chloroplasts have outer membrane proteins (OMPs) that perform many fundamental biological processes. The OMPs in Gram-negative bacteria are inserted and folded into the outer membrane by the β-barrel assembly machinery (BAM). The mechanism involved is poorly understood, owing to the absence of a structure of the entire BAM complex. Here we report two crystal structures of the Escherichia coli BAM complex in two distinct states: an inward-open state and a lateral-open state. Our structures reveal that the five polypeptide transport-associated domains of BamA form a ring architecture with four associated lipoproteins, BamB-BamE, in the periplasm. Our structural, functional studies and molecular dynamics simulations indicate that these subunits rotate with respect to the integral membrane β-barrel of BamA to induce movement of the β-strands of the barrel and promote insertion of the nascent OMP.

PubMed: 26901871
DOI: 10.1038/nature17199

Experimental method

X-RAY DIFFRACTION (3.5 Å)