Analysis of the outer membrane BAM complex

革兰氏阴性菌需要BAM复合体将膜蛋白插入外膜。这个重要的复合体由五种蛋白质组成，大的跨膜桶是BamA。BamA在其N端携带5个POTRA结构域，这些结构域与复合物中的其他蛋白质相互作用。只有BamA和BamD是必需的，但这些蛋白质的作用尚不清楚。我们解决了外膜蛋白Hbp的晶体结构，并研究了BamC和BamD之间的相互作用。Hbp β -桶是BAM的底物，但两者之间的相互作用尚不清楚。我们已经证明BamC和BamD相互作用产生了一个灵活的配合物。

Gram negative bacteria require the BAM complex for the insertion of membrane proteins into the outer membrane. This essential complex consists of five proteins, the large transmembrane barrel being BamA. BamA carries five POTRA domains at its N terminus which interact with other proteins in the complex. Only BamA and BamD are essential, but the roles of these proteins is unknown. We have solved the crystal structure of an outer membrane protein, Hbp, and studied the interaction between BamC and BamD. The Hbp beta-barrel is a substrate of BAM, but the interactions between the two are unclear. We have shown that BamC and BamD interact to give a flexible complex.