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Structural basis for the interaction of BamB with the POTRA3–4 domains of BamA
Author(s) -
Chen Zhen,
Zhan Li-Hong,
Hou Hai-Feng,
Gao Zeng-Qiang,
Xu Jian-Hua,
Dong Cheng,
Dong Yu-Hui
Publication year - 2016
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798315024729
Subject(s) - bama , basis (linear algebra) , biology , mathematics , genetics , geometry , escherichia coli , bacterial outer membrane , gene
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.