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Instruments / Technical Area	Publication Details	Published	Actions
I04-1-Macromolecular Crystallography (fixed wavelength)	BamA β6C strand and periplasmic turns are critical for outer membrane protein insertion and assembly Yinghong Gu , Yi Zeng , Zhongshan Wang , Changjiang Dong Biochemical Journal DOI: 10.1042/BCJ20170636 Diamond Proposal Number(s): [9475] Show Abstract ▼ Abstract: Outer membrane β-barrel proteins play important roles in importing nutrients, exporting wastes and conducting signals in Gram-negative bacteria, mitochondria and chloroplasts. The outer membrane proteins are inserted and assembled into the outer membrane by OMP85 family proteins. In Escherichia coli , the b-barrel assembly machinery (BAM) contains four lipoproteins BamB, BamC, BamD and BamE, and one outer membrane protein BamA, forming a "top hat"-like structure. Structural and functional studies of the E. coli BAM machinery have revealed that the rotation of periplasmic ring may trigger the barrel b1C-b6C scissor-like movement that promote the unfolded outer membrane protein insertion without using ATP. Here we report the BamA C-terminal barrel structure of Salmonella enterica Typhimurium str. LT2 and functional assays, which reveal that the BamA's C-terminal residue Trp, the b16C strand of the barrel and the periplasmic turns are critical for the functionality of BamA. These findings indicate that the unique b16C and the periplasmic turns of BamA are important for the out membrane insertion and assembly. The periplasmic turns might mediate the rotation of the periplasmic ring to the scissor-like movement of BamA b1C-b6C, triggering the outer membrane protein insertion. These results are important for understanding the outer membrane protein insertion in Gram-negative bacteria, as well as in mitochondria and chloroplasts.	Oct 2017
I02-Macromolecular Crystallography I03-Macromolecular Crystallography I04-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Structural basis for outer membrane lipopolysaccharide insertion Haohao Dong , Quanju Xiang , Yinghong Gu , Zhongshan Wang , Neil Paterson , Phillip J. Stansfeld , Chuan He , Yizheng Zhang , Wenjian Wang , Changjiang Dong Nature 511 (7507), 52 - 56 DOI: 10.1038/nature13464 PMID: 24990744 Diamond Proposal Number(s): [7641] Show Abstract ▼ Abstract: Lipopolysaccharide (LPS) is essential for most Gram-negative bacteria and has crucial roles in protection of the bacteria from harsh environments and toxic compounds, including antibiotics. Seven LPS transport proteins (that is, LptALptG) form a trans-envelope protein complex responsible for the transport of LPS from the inner membrane to the outer membrane, the mechanism for which is poorly understood. Here we report the first crystal structure of the unique integral membrane LPS translocon LptDLptE complex. LptD forms a novel 26-stranded β-barrel, which is to our knowledge the largest β-barrel reported so far. LptE adopts a roll-like structure located inside the barrel of LptD to form an unprecedented two-protein barrel and plug architecture. The structure, molecular dynamics simulations and functional assays suggest that the hydrophilic O-antigen and the core oligosaccharide of the LPS may pass through the barrel and the lipid A of the LPS may be inserted into the outer leaflet of the outer membrane through a lateral opening between strands β1 and β26 of LptD. These findings not only help us to understand important aspects of bacterial outer membrane biogenesis, but also have significant potential for the development of novel drugs against multi-drug resistant pathogenic bacteria.	Jun 2014

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