| Literature DB >> 26394220 |
Patrick K O'Neil1, Sarah E Rollauer2, Nicholas Noinaj1, Susan K Buchanan2.
Abstract
β-Barrel membrane proteins are found in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria; however, exactly how they are folded and inserted remains unknown. Over the past decade, both functional and structural studies have greatly contributed to addressing this elusive mechanism. It is known that a conserved core machinery is required for each organelle, though the overall composition varies significantly. The vast majority of studies that aimed to understand the biogenesis of β-barrel membrane proteins has been conducted in Gram-negative bacteria. Here, it is the task of a multicomponent complex known as the β-barrel assembly machinery (BAM) complex to fold and insert new β-barrel membrane proteins into the outer membrane. In this review, we will discuss recent discoveries with the goal of utilizing all reported structural and functional studies to piece together a current structural model for the fully assembled BAM complex.Entities:
Mesh:
Substances:
Year: 2015 PMID: 26394220 PMCID: PMC4631317 DOI: 10.1021/acs.biochem.5b00852
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162