
doi: 10.1038/nrmicro2069
pmid: 19182809
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.
Models, Molecular, Crystal-Structure, Protein Folding, Escherichia coli Proteins, Bacterial Protein, 2400 Immunology and Microbiology, Beta-Barrel Proteins, Cytoplasmic Membrane, Yaet Complex, Protein Transport, Chaperone Activity, Functional Domains, Lipid Export, Secretin Puld, Gram-Negative Bacteria, Protein Multimerization, Escherichia-Coli, Bacterial Outer Membrane Proteins, Molecular Chaperones
Models, Molecular, Crystal-Structure, Protein Folding, Escherichia coli Proteins, Bacterial Protein, 2400 Immunology and Microbiology, Beta-Barrel Proteins, Cytoplasmic Membrane, Yaet Complex, Protein Transport, Chaperone Activity, Functional Domains, Lipid Export, Secretin Puld, Gram-Negative Bacteria, Protein Multimerization, Escherichia-Coli, Bacterial Outer Membrane Proteins, Molecular Chaperones
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