8RT9
Stalk complex full-length structure (TrwJ/VirB5-TrwI/VirB6) from the fully-assembled R388 type IV secretion system determined by cryo-EM.
Summary for 8RT9
| Entry DOI | 10.2210/pdb8rt9/pdb |
| EMDB information | 19483 |
| Descriptor | TrwJ protein, TrwI protein (2 entities in total) |
| Functional Keywords | type iv secretion system type 4 secretion system t4ss stalk r388 plasmid conjugation bacterial secretion secretion secretion system protein complex virb5 virb6 trwi trwj, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 10 |
| Total formula weight | 302573.16 |
| Authors | Mace, K.,Waksman, G. (deposition date: 2024-01-25, release date: 2024-06-19, Last modification date: 2024-08-14) |
| Primary citation | Mace, K.,Waksman, G. Cryo-EM structure of a conjugative type IV secretion system suggests a molecular switch regulating pilus biogenesis. Embo J., 43:3287-3306, 2024 Cited by PubMed Abstract: Conjugative type IV secretion systems (T4SS) mediate bacterial conjugation, a process that enables the unidirectional exchange of genetic materials between a donor and a recipient bacterial cell. Bacterial conjugation is the primary means by which antibiotic resistance genes spread among bacterial populations (Barlow 2009; Virolle et al, 2020). Conjugative T4SSs form pili: long extracellular filaments that connect with recipient cells. Previously, we solved the cryo-electron microscopy (cryo-EM) structure of a conjugative T4SS. In this article, based on additional data, we present a more complete T4SS cryo-EM structure than that published earlier. Novel structural features include details of the mismatch symmetry within the OMCC, the presence of a fourth VirB8 subunit in the asymmetric unit of both the arches and the inner membrane complex (IMC), and a hydrophobic VirB5 tip in the distal end of the stalk. Additionally, we provide previously undescribed structural insights into the protein VirB10 and identify a novel regulation mechanism of T4SS-mediated pilus biogenesis by this protein, that we believe is a key checkpoint for this process. PubMed: 38886579DOI: 10.1038/s44318-024-00135-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.97 Å) |
Structure validation
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