Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel

• Published in: Nature communications Vol. 10; no. 1; pp. 3358 - 13
• Main Authors: Doyle, Matthew T., Bernstein, Harris D.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 26.07.2019; Nature Publishing Group; Nature Portfolio
• Subjects: 631/326; 631/45; 631/57; 82/1; 82/29; 82/80; Assembly; Bacterial Outer Membrane Proteins - chemistry; Bacterial Outer Membrane Proteins - genetics; Bacterial Outer Membrane Proteins - metabolism; Cell Membrane - chemistry; Cell Membrane - genetics; Cell Membrane - metabolism; Crosslinking; E coli; Escherichia coli - chemistry; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Humanities and Social Sciences; Integration; Lipids; Membrane proteins; multidisciplinary; Outer membrane proteins; Polypeptides; Protein Binding; Protein Domains; Proteins; Science; Science (multidisciplinary); Substrates

The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). The central BAM subunit (BamA) itself contains a β-barrel domain that is essential for OM protein biogenesis, but its mechanism of action is unknown. To elucidate its fu...