7BNQ
Lateral-closed conformation of the lid-locked BAM complex (BamA E435C S665C, BamBDCE) by cryoEM
Summary for 7BNQ
| Entry DOI | 10.2210/pdb7bnq/pdb |
| Related | 7BM5 |
| EMDB information | 12232 |
| 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 assembly, beta-barrel, gram negative bacteria, protein foldase, membrane protein |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 5 |
| Total formula weight | 210784.18 |
| Authors | Haysom, S.F. (deposition date: 2021-01-22, release date: 2021-06-02, Last modification date: 2024-10-16) |
| Primary citation | White, P.,Haysom, S.F.,Iadanza, M.G.,Higgins, A.J.,Machin, J.M.,Whitehouse, J.M.,Horne, J.E.,Schiffrin, B.,Carpenter-Platt, C.,Calabrese, A.N.,Storek, K.M.,Rutherford, S.T.,Brockwell, D.J.,Ranson, N.A.,Radford, S.E. The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding. Nat Commun, 12:4174-4174, 2021 Cited by PubMed Abstract: 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. PubMed: 34234105DOI: 10.1038/s41467-021-24432-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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