title: Structure of Escherichia coli BamB and its interaction with POTRA domains of BamA.
abstract: In Escherichia coli, the BAM complex is essential for the assembly and insertion of outer membrane proteins (OMPs). The BAM complex is comprised of an integral β-barrel outer membrane protein BamA and four accessory lipoproteins BamB, BamC, BamD and BamE. Here, the crystal structure of BamB is reported. The crystal of BamB diffracted to 2.0 Å with one monomer in the asymmetric unit and the structure is composed of eight-bladed β-propeller motifs. Pull-down and Western blotting assays indicate that BamB interacts directly with the POTRA 1-3 domain of BamA and the C-terminal region of the POTRA 1-3 domain plays an important role in the interaction, while the POTRA 1-2 domain is not required for the interaction.
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, People's Republic of China.
authors.forename: Cheng
authors.initials: C
authors.lastname: Dong
authors.forename: Xue
authors.initials: X
authors.lastname: Yang
authors.forename: Hai-Feng
authors.initials: HF
authors.lastname: Hou
authors.forename: Yue-Quan
authors.initials: YQ
authors.lastname: Shen
authors.forename: Yu-Hui
authors.initials: YH
authors.lastname: Dong
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D040681:Structural Homology, Protein
chemical_list: D001425:Bacterial Outer Membrane Proteins; C503914:BamA protein, E coli; C557407:BamB protein, E coli; D029968:Escherichia coli Proteins