Structural basis for lipopolysaccharide insertion in the bacterial outer membrane, Nature, Published online 18 June 2014
发布时间：2014年06月20日
Nature, Published online 18 June 2014, doi:10.1038/nature1348
Structural basis for lipopolysaccharide insertion in the bacterial outer membrane
Shuai Qiao,1, 2, Qingshan Luo,1, 2, Yan Zhao,1, 3, Xuejun Cai Zhang1, & Yihua Huang1
Abstract
One of the fundamental properties of biological membranes is the asymmetric distribution of membrane lipids. In Gram-negative bacteria, the outer leaflet of the outer membrane is composed predominantly of lipopolysaccharides (LPS)1. The export of LPS requires seven essential lipopolysaccharide transport (Lpt) proteins to move LPS from the inner membrane, through the periplasm to the surface2. Of the seven Lpt proteins, the LptD–LptE complex is responsible for inserting LPS into the external leaflet of the outer membrane3, 4. Here we report the crystal structure of the ~110-kilodalton membrane protein complex LptD–LptE from Shigella flexneri at 2.4 angstrom resolution. The structure reveals an unprecedented two-protein plug-and-barrel architecture with LptE embedded into a 26-stranded β-barrel formed by LptD. Importantly, the secondary structures of the first two β-strands are distorted by two proline residues, weakening their interactions with neighbouring β-strands and creating a potential portal on the barrel wall that could allow lateral diffusion of LPS into the outer membrane. The crystal structure of the LptD–LptE complex opens the door to new antibiotic strategies targeting the bacterial outer membrane.
附件下载：
Structural basis for lipopolysaccharide insertion in the bacterial outer membrane, Nature, Published online 18 June 2014
Nature, Published online 18 June 2014, doi:10.1038/nature1348
Structural basis for lipopolysaccharide insertion in the bacterial outer membrane
Shuai Qiao,1, 2, Qingshan Luo,1, 2, Yan Zhao,1, 3, Xuejun Cai Zhang1, & Yihua Huang1
Abstract
One of the fundamental properties of biological membranes is the asymmetric distribution of membrane lipids. In Gram-negative bacteria, the outer leaflet of the outer membrane is composed predominantly of lipopolysaccharides (LPS)1. The export of LPS requires seven essential lipopolysaccharide transport (Lpt) proteins to move LPS from the inner membrane, through the periplasm to the surface2. Of the seven Lpt proteins, the LptD–LptE complex is responsible for inserting LPS into the external leaflet of the outer membrane3, 4. Here we report the crystal structure of the ~110-kilodalton membrane protein complex LptD–LptE from Shigella flexneri at 2.4 angstrom resolution. The structure reveals an unprecedented two-protein plug-and-barrel architecture with LptE embedded into a 26-stranded β-barrel formed by LptD. Importantly, the secondary structures of the first two β-strands are distorted by two proline residues, weakening their interactions with neighbouring β-strands and creating a potential portal on the barrel wall that could allow lateral diffusion of LPS into the outer membrane. The crystal structure of the LptD–LptE complex opens the door to new antibiotic strategies targeting the bacterial outer membrane.
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文章链接：http://www.nature.com/nature/journal/vaop/ncurrent/full/nature13484.html