7O42
TrwK/VirB4unbound trimer of dimers complex (with Hcp1) from the R388 type IV secretion system determined by cryo-EM.
This is a non-PDB format compatible entry.
Summary for 7O42
| Entry DOI | 10.2210/pdb7o42/pdb |
| EMDB information | 12716 |
| Descriptor | TrwK protein,Protein hcp1 (1 entity in total) |
| Functional Keywords | type iv secretion system, type 4 secretion system, t4ss, inner membrane complex, inner membrane, r388 plasmid, conjugation, atpase, bacterial secretion, secretion, secretion system, protein complex, virb4, trwk, hcp, membrane protein |
| Biological source | Salmonella dublin More |
| Total number of polymer chains | 6 |
| Total formula weight | 668927.06 |
| Authors | Vadakkepat, A.K.,Mace, K.,Lukoyanova, N.,Waksman, G. (deposition date: 2021-04-04, release date: 2022-06-22, Last modification date: 2024-07-10) |
| Primary citation | Mace, K.,Vadakkepat, A.K.,Redzej, A.,Lukoyanova, N.,Oomen, C.,Braun, N.,Ukleja, M.,Lu, F.,Costa, T.R.D.,Orlova, E.V.,Baker, D.,Cong, Q.,Waksman, G. Cryo-EM structure of a type IV secretion system. Nature, 607:191-196, 2022 Cited by PubMed Abstract: Bacterial conjugation is the fundamental process of unidirectional transfer of DNAs, often plasmid DNAs, from a donor cell to a recipient cell. It is the primary means by which antibiotic resistance genes spread among bacterial populations. In Gram-negative bacteria, conjugation is mediated by a large transport apparatus-the conjugative type IV secretion system (T4SS)-produced by the donor cell and embedded in both its outer and inner membranes. The T4SS also elaborates a long extracellular filament-the conjugative pilus-that is essential for DNA transfer. Here we present a high-resolution cryo-electron microscopy (cryo-EM) structure of a 2.8 megadalton T4SS complex composed of 92 polypeptides representing 8 of the 10 essential T4SS components involved in pilus biogenesis. We added the two remaining components to the structural model using co-evolution analysis of protein interfaces, to enable the reconstitution of the entire system including the pilus. This structure describes the exceptionally large protein-protein interaction network required to assemble the many components that constitute a T4SS and provides insights on the unique mechanism by which they elaborate pili. PubMed: 35732732DOI: 10.1038/s41586-022-04859-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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