8QPU
Release Complex: BAM bound EspP and Extended SurA
Summary for 8QPU
| Entry DOI | 10.2210/pdb8qpu/pdb |
| Related | 8PZ1 8PZ2 8PZU 8PZV 8Q05 8QP5 |
| EMDB information | 18034 18035 18045 18046 18053 18543 18562 |
| Descriptor | Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamD, ... (7 entities in total) |
| Functional Keywords | outer membrane, complex, chaperone, protein folding, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 7 |
| Total formula weight | 289441.29 |
| Authors | |
| Primary citation | Fenn, K.L.,Horne, J.E.,Crossley, J.A.,Bohringer, N.,Horne, R.J.,Schaberle, T.F.,Calabrese, A.N.,Radford, S.E.,Ranson, N.A. Outer membrane protein assembly mediated by BAM-SurA complexes. Nat Commun, 15:7612-7612, 2024 Cited by PubMed Abstract: The outer membrane is a formidable barrier that protects Gram-negative bacteria against environmental threats. Its integrity requires the correct folding and insertion of outer membrane proteins (OMPs) by the membrane-embedded β-barrel assembly machinery (BAM). Unfolded OMPs are delivered to BAM by the periplasmic chaperone SurA, but how SurA and BAM work together to ensure successful OMP delivery and folding remains unclear. Here, guided by AlphaFold2 models, we use disulphide bond engineering in an attempt to trap SurA in the act of OMP delivery to BAM, and solve cryoEM structures of a series of complexes. The results suggest that SurA binds BAM at its soluble POTRA-1 domain, which may trigger conformational changes in both BAM and SurA that enable transfer of the unfolded OMP to the BAM lateral gate for insertion into the outer membrane. Mutations that disrupt the interaction between BAM and SurA result in outer membrane assembly defects, supporting the key role of SurA in outer membrane biogenesis. PubMed: 39218969DOI: 10.1038/s41467-024-51358-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.2 Å) |
Structure validation
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