| Literature DB >> 26894671 |
Zhen Chen1, Li Hong Zhan1, Hai Feng Hou1, Zeng Qiang Gao1, Jian Hua Xu1, Cheng Dong1, Yu Hui Dong1.
Abstract
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.Entities:
Keywords: BamB; POTRA domains; assembly and insertion; crystal structure; outer membrane proteins
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Year: 2016 PMID: 26894671 DOI: 10.1107/S2059798315024729
Source DB: PubMed Journal: Acta Crystallogr D Struct Biol ISSN: 2059-7983 Impact factor: 7.652