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-Structure paper
タイトル | The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 4174, Year 2021 |
掲載日 | 2021年7月7日 |
著者 | Paul White / Samuel F Haysom / Matthew G Iadanza / Anna J Higgins / Jonathan M Machin / James M Whitehouse / Jim E Horne / Bob Schiffrin / Charlotte Carpenter-Platt / Antonio N Calabrese / Kelly M Storek / Steven T Rutherford / David J Brockwell / Neil A Ranson / Sheena E Radford / |
PubMed 要旨 | The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit ...The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit BamA assists in OMP folding, and the contribution of membrane disruption to BAM catalysis remain unresolved. Here, we use an anti-BamA monoclonal antibody fragment (Fab1) and two disulphide-crosslinked BAM variants (lid-locked (LL), and POTRA-5-locked (P5L)) to dissect these roles. Despite being lethal in vivo, we show that all complexes catalyse folding in vitro, albeit less efficiently than wild-type BAM. CryoEM reveals that while Fab1 and BAM-P5L trap an open-barrel state, BAM-LL contains a mixture of closed and contorted, partially-open structures. Finally, all three complexes globally destabilise the lipid bilayer, while BamA does not, revealing that the BAM lipoproteins are required for this function. Together the results provide insights into the role of BAM structure and lipid dynamics in OMP folding. |
リンク | Nat Commun / PubMed:34234105 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.95 - 10.3 Å |
構造データ | EMDB-12232, PDB-7bnq: EMDB-12262, PDB-7nbx: EMDB-12263: EMDB-12271, PDB-7ncs: EMDB-12272, PDB-7nd0: PDB-7bm5: |
由来 |
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キーワード | IMMUNE SYSTEM / Antibody / antibiotic / Fab / BamA / MEMBRANE PROTEIN / Outer membrane protein assembly / beta-barrel / Gram negative bacteria / protein foldase |