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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA
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Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA

机译:BamB之间的相互作用的结构基础巴马的POTRA3-4域

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摘要

In Escherichia coli, the Omp85 protein BamA and four lipoproteins (BamBCDE) constitute the BAMcomplex, which is essential for the assembly and insertion of outer membrane proteins into the outer membrane. Here, the crystal structure of BamB in complex with the POTRA3-4 domains of BamA is reported at 2.1 angstrom resolution. Based on this structure, the POTRA3 domain is associated with BamB via hydrogen-bonding and hydrophobic interactions. Structural and biochemical analysis revealed that the conserved residues Arg77, Glu127, Glu150, Ser167, Leu192, Leu194 and Arg195 of BamB play an essential role in interaction with the POTRA3 domain.
机译:在大肠杆菌中,Omp85巴马和蛋白质四个脂蛋白(BamBCDE)构成的组装BAMcomplex,这是至关重要的和外膜蛋白插入外膜。BamB在复杂的巴马POTRA3-4域据报道为2.1埃分辨率。这个结构,POTRA3域相关联BamB通过氢键和疏水交互。守恒的残留Arg77透露,Glu127 Glu150、Ser167 Leu192 Leu194 and Arg195的BamB互动起着关键作用POTRA3域。

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