8BWC
E. coli BAM complex (BamABCDE) wild-type
Summary for 8BWC
| Entry DOI | 10.2210/pdb8bwc/pdb |
| EMDB information | 16282 |
| Descriptor | Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, ... (5 entities in total) |
| Functional Keywords | outer membrane protein, protein folding, beta barrel, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 5 |
| Total formula weight | 200226.02 |
| Authors | Machin, J.M.,Radford, S.E.,Ranson, N.A. (deposition date: 2022-12-06, release date: 2023-05-24, Last modification date: 2023-09-06) |
| Primary citation | Haysom, S.F.,Machin, J.,Whitehouse, J.M.,Horne, J.E.,Fenn, K.,Ma, Y.,El Mkami, H.,Bohringer, N.,Schaberle, T.F.,Ranson, N.A.,Radford, S.E.,Pliotas, C. Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells. Angew.Chem.Int.Ed.Engl., 62:e202218783-e202218783, 2023 Cited by PubMed Abstract: The β-barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram-negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but all have been obtained under conditions which lack the unique features and complexity of the outer membrane (OM). Here, we use Pulsed Electron-Electron Double Resonance (PELDOR, or DEER) spectroscopy distance measurements to interrogate the conformational ensemble of the BAM complex in E. coli cells. We show that BAM adopts a broad ensemble of conformations in the OM, while in the presence of the antibiotic darobactin B (DAR-B), BAM's conformational equilibrium shifts to a restricted ensemble consistent with the lateral closed state. Our in-cell PELDOR findings are supported by new cryoEM structures of BAM in the presence and absence of DAR-B. This work demonstrates the utility of PELDOR to map conformational changes in BAM within its native cellular environment. PubMed: 37162386DOI: 10.1002/anie.202218783 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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