7Q1V
Arches protomer (trimer of TrwG/VirB8peri) structure from the fully-assembled R388 type IV secretion system determined by cryo-EM.
Summary for 7Q1V
| Entry DOI | 10.2210/pdb7q1v/pdb |
| EMDB information | 12709 12933 13767 |
| Descriptor | TrwG protein (1 entity in total) |
| Functional Keywords | type iv secretion system, type 4 secretion system, t4ss, imc, inner membrane complex, inner membrane, arches, stalk, periplasmic, r388 plasmid, conjugation, bacterial secretion, secretion, secretion system, protein complex, virb3, virb4, virb5, virb6, virb8, trwm, trwk, trwj, trwi, trwg, membrane protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 3 |
| Total formula weight | 77399.98 |
| Authors | Mace, K.,Vadakkepat, A.K.,Lukoyanova, N.,Waksman, G. (deposition date: 2021-10-21, release date: 2022-06-22, Last modification date: 2024-07-17) |
| 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 (6.18 Å) |
Structure validation
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