Literature DB >> 26894671

Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA.

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

Mesh:

Substances:

Year:  2016        PMID: 26894671     DOI: 10.1107/S2059798315024729

Source DB:  PubMed          Journal:  Acta Crystallogr D Struct Biol        ISSN: 2059-7983            Impact factor:   7.652


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  6 in total

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