 Hi, my name is Kelly and this video is an overview of the review article that we just published in the latest issue of protein science. In this review, we summarized the latest structural and functional information that's available on the beta-barrel assembly machinery complex, which is more often more simply known as the BAM complex. The BAM complex is an essential as well as a very well-conserved outer membrane protein complex that's found in the outer membrane of all known gram-negative bacteria. In gram-negative bacteria, the outer membrane basically serves as a physical barrier to protect the cells against its surroundings. You can also think of the outer membrane as a molecular sieve that controls the traffic of molecules into and out of the cell. Many of these functions are carried out by the proteins that are found in the outer membrane that are collectively known as the outer membrane proteins, or ALMS. Different ALMS have different functions, but they all have a transmembrane beta-barrel domain. These beta-barrel domains consist of 8 to 24 anti-parallel beta strands that are arranged in a barrel shape, which sits in the membrane. In order for these ALMS to be functional, they must first be properly folded and inserted into the outer membrane. And this process is catalyzed by the BAM complex. In E. coli, the BAM complex consists of five proteins, M, A, E, C, D and E. BAM A is an ALMS itself, as it has a beta-barrel domain, but it also has a region that extends into the periplasm. BAM B, C, D and E are lipoproteins which exist in the periplasm, but are found anchored to the outer membrane. It's not yet clear how this complex functions, but a number of recent studies have provided interesting insights. For example, we're starting to understand how the different components of the BAM complex may interact with each other and also with the ALMS substrate. We now also know what the complex may look like, thanks to structural studies. There are already multiple structures solved for the periplasm region of BAM A. Then last year in 2011, the structures became available for BAM E, BAM B, BAM C, BAM D, and most recently BAM C, the EXOP complex. How the BAM complex functions is still a mystery, but several models have been proposed. One model proposes that the ALMS substrate translocates through the pore of BAM A and inserts into the membrane from the extracellular face. Another model suggests that the ALMS may insert into the membrane from the periprosmic face. A third model proposes a similar mechanism, but suggests that a tetramer of BAM A may be present. In this review, we propose a new model. We propose that the ALMS may use BAM A as a template and fold as an extension of BAM A and then bought off to become an independent barrel. But there's still a lot of work that needs to be done to understand the exact mechanism of the BAM complex. Because the antibiotic resistance is a growing problem, researchers are constantly looking for new drug targets. The BAM complex is an ideal candidate because it's essential and it's located in the outer membrane. So there's a lot of exciting research going on in this field right now, and we invite you to read our review and get up to date with all the latest findings.