Dong Cheng, Yang Xue, Hou Hai-Feng, Shen Yue-Quan, Dong Yu-Hui
State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, People's Republic of China.
Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1134-9. doi: 10.1107/S0907444912023141. Epub 2012 Aug 18.
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.
在大肠杆菌中，BAM复合物对于外膜蛋白（OMPs）的组装和插入至关重要。BAM复合物由一个整合的β-桶状外膜蛋白BamA和四个辅助脂蛋白BamB、BamC、BamD和BamE组成。在此，报道了BamB的晶体结构。BamB的晶体衍射至2.0 Å，不对称单元中有一个单体，其结构由八叶β-螺旋桨基序组成。下拉和蛋白质印迹分析表明，BamB与BamA的POTRA 1-3结构域直接相互作用，且POTRA 1-3结构域的C末端区域在这种相互作用中起重要作用，而相互作用不需要POTRA 1-2结构域。
