8S6H
Cryo-EM Structure of the R388 plasmid conjugative pilus reveals a helical polymer characterised by an unusual pilin/phospholipid binary complex
This is a non-PDB format compatible entry.
Summary for 8S6H
| Entry DOI | 10.2210/pdb8s6h/pdb |
| Related | 5LEG 7JSV 8CW4 8EXH |
| EMDB information | 19758 |
| Descriptor | TrwL protein, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE (2 entities in total) |
| Functional Keywords | conjugal transfer protein, virb2, conjugative pilus, type-4 secretion system fibre, conduit for horizontal gene transfer, anti-microbial resistance, protein fibril |
| Biological source | Escherichia coli HB101 |
| Total number of polymer chains | 69 |
| Total formula weight | 560259.44 |
| Authors | Vadakkepat, A.K.,Waksman, G.,Redzej, A. (deposition date: 2024-02-27, release date: 2024-07-24, Last modification date: 2024-09-18) |
| Primary citation | Vadakkepat, A.K.,Xue, S.,Redzej, A.,Smith, T.K.,Ho, B.T.,Waksman, G. Cryo-EM structure of the R388 plasmid conjugative pilus reveals a helical polymer characterized by an unusual pilin/phospholipid binary complex. Structure, 32:1335-, 2024 Cited by PubMed Abstract: Bacterial conjugation is a process by which DNA is transferred unidirectionally from a donor cell to a recipient cell. It is the main means by which antibiotic resistance genes spread among bacterial populations. It is crucially dependent upon the elaboration of an extracellular appendage, termed "pilus," by a large double-membrane-spanning secretion system termed conjugative "type IV secretion system." Here we present the structure of the conjugative pilus encoded by the R388 plasmid. We demonstrate that, as opposed to all conjugative pili produced so far for cryoelectron microscopy (cryo-EM) structure determination, the conjugative pilus encoded by the R388 plasmid is greatly stimulated by the presence of recipient cells. Comparison of its cryo-EM structure with existing conjugative pilus structures highlights a number of important differences between the R388 pilus structure and that of its homologs, the most prominent being the highly distinctive conformation of its bound lipid. PubMed: 39002540DOI: 10.1016/j.str.2024.06.009 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.39 Å) |
Structure validation
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