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I02-Macromolecular Crystallography I03-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Structural basis of outer membrane protein insertion by the BAM complex Yinghong Gu , Huanyu Li , Haohao Dong , Yi Zeng , Zhengyu Zhang , Neil G. Paterson , Phillip J. Stansfeld , Zhongshan Wang , Yizheng Zhang , Wenjian Wang , Changjiang Dong Nature 531, 64 - 69 DOI: 10.1038/nature17199 Diamond Proposal Number(s): [9475] Show Abstract ▼ 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.	Feb 2016

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