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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Crystal structure of the outer membrane protein OmpU from Vibrio cholerae Vibrio cholerae at 2.2?? resolution
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Crystal structure of the outer membrane protein OmpU from Vibrio cholerae Vibrio cholerae at 2.2?? resolution

机译:外膜蛋白的晶体结构从霍乱弧菌OmpU霍乱弧菌2.2 ? ?

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摘要

Vibrio cholerae causes a severe disease that kills thousands of people annually. The outer membrane protein OmpU is the most abundant outer membrane protein in V. cholerae , and has been identified as an important virulence factor that is involved in host‐cell interaction and recognition, as well as being critical for the survival of the pathogenic V. cholerae in the host body and in harsh environments. The mechanism of these processes is not well understood owing to a lack of the structure of V. cholerae OmpU. Here, the crystal structure of the V. cholerae OmpU trimer is reported to a resolution of 2.2??. The protomer forms a 16‐β‐stranded barrel with a noncanonical N‐terminal coil located in the lumen of the barrel that consists of residues Gly32–Ser42 and is observed to participate in forming the second gate in the pore. By mapping the published functional data onto the OmpU structure, the OmpU structure reinforces the notion that the long extracellular loop L4 with a β‐hairpin‐like motif may be critical for host‐cell binding and invasion, while L3, L4 and L8 are crucially implicated in phage recognition by V. cholerae .
机译:霍乱弧菌引起一种严重的疾病每年成千上万的人。蛋白质OmpU是最丰富的外膜蛋白质在霍乱弧菌,已被确认作为一个重要的毒力因子在宿主细胞相互作用和识别中,是生存的关键宿主的身体和霍乱弧菌致病恶劣的环境。由于缺乏过程不是很好理解霍乱弧菌OmpU的结构。晶体结构的霍乱弧菌OmpU三聚物据报道,分辨率为2.2 ? ?。原体形成一个16β链桶与不在经典里的N端线圈位于腔由残留的桶Gly32-Ser42观察参与孔隙形成第二个门。数据到OmpU发布的功能结构,OmpU结构强化了长细胞外循环L4的说法β发夹的类主题可能是至关重要的宿主细胞绑定和应承担的入侵,而L3、L4和18都有至关重要的涉及噬菌体的认可由霍乱弧菌。

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