Membrane protein architects: the role of the BAM complex in outer membrane protein assembly.
The folding of transmembrane proteins into the outer membrane presents formidable challenges to Gram-negative bacteria. These proteins must migrate from the cytoplasm, through the inner membrane and into the periplasm, before being recognized by the beta-barrel assembly machinery, which mediates efficient insertion of folded beta-barrels into the outer membrane. Recent discoveries of component structures and accessory interactions of this complex are yielding insights into how cells fold membrane proteins. Here, we discuss how these structures illuminate the mechanisms responsible for the biogenesis of outer membrane proteins.
Knowles
Timothy J
TJ
Cancer Research UK Institute for Cancer Studies, School of Cancer Sciences, Edgbaston, Birmingham, UK.
Scott-Tucker
Anthony
A
Overduin
Michael
M
Henderson
Ian R
IR
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D006090:Gram-Negative Bacteria / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding; D055503:Protein Multimerization; D021381:Protein Transport
D001425:Bacterial Outer Membrane Proteins; C503914:BamA protein, E coli; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones