巴马
基础(线性代数)
生物
数学
遗传学
几何学
大肠杆菌
细菌外膜
基因
作者
Zhen Chen,Li-Hong Zhan,Haifeng Hou,Zengqiang Gao,Jian-Hua Xu,Dong Cheng,Yuhui Dong
标识
DOI:10.1107/s2059798315024729
摘要
In Escherichia coli, the Omp85 protein BamA and four lipoproteins (BamBCDE) constitute the BAM complex, 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 Å 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.
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