5LJO
E. coli BAM complex (BamABCDE) by cryoEM
Summary for 5LJO
| Entry DOI | 10.2210/pdb5ljo/pdb |
| EMDB information | 4061 |
| Descriptor | Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, Outer membrane protein assembly factor BamD, ... (5 entities in total) |
| Functional Keywords | membrane protein, bam, omp, beta barrel, outer membrane, gram negative |
| Biological source | Escherichia coli K12 More |
| Cellular location | Cell outer membrane ; Lipid-anchor : P77774 P0A903 P0AC04 P0A938 Cell outer membrane : B7MBF8 |
| Total number of polymer chains | 5 |
| Total formula weight | 180072.79 |
| Authors | Iadanza, M.G.,Ranson, N.A.,Radford, S.E.,Higgins, A.J.,Schffrin, B.,Calabrese, A.N.,Ashcroft, A.E.,Brockwell, D.J. (deposition date: 2016-07-19, release date: 2016-10-12, Last modification date: 2024-05-08) |
| Primary citation | Iadanza, M.G.,Higgins, A.J.,Schiffrin, B.,Calabrese, A.N.,Brockwell, D.J.,Ashcroft, A.E.,Radford, S.E.,Ranson, N.A. Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM. Nat Commun, 7:12865-12865, 2016 Cited by PubMed Abstract: The β-barrel assembly machinery (BAM) is a ∼203 kDa complex of five proteins (BamA-E), which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel proteins into the outer membrane via a poorly understood mechanism. Several current models suggest that BAM functions through a 'lateral gating' motion of the β-barrel of BamA. Here we present a cryo-EM structure of the BamABCDE complex, at 4.9 Å resolution. The structure is in a laterally open conformation showing that gating is independent of BamB binding. We describe conformational changes throughout the complex and interactions between BamA, B, D and E, and the detergent micelle that suggest communication between BAM and the lipid bilayer. Finally, using an enhanced reconstitution protocol and functional assays, we show that for the outer membrane protein OmpT, efficient folding in vitro requires lateral gating in BAM. PubMed: 27686148DOI: 10.1038/ncomms12865 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.9 Å) |
Structure validation
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