7OKN
Structure of the outer-membrane core complex (inner ring) from a conjugative type IV secretion system
Summary for 7OKN
| Entry DOI | 10.2210/pdb7okn/pdb |
| EMDB information | 12962 |
| Descriptor | TraB, Type IV conjugative transfer system lipoprotein TraV (2 entities in total) |
| Functional Keywords | type iv secretion system, f plasmid, outer-membrane core complex, conjugation, membrane protein |
| Biological source | Salmonella enterica More |
| Total number of polymer chains | 34 |
| Total formula weight | 1185422.78 |
| Authors | Amin, H.,Ilangovan, A.,Costa, T.R.D. (deposition date: 2021-05-18, release date: 2021-12-01, Last modification date: 2024-10-23) |
| Primary citation | Amin, H.,Ilangovan, A.,Costa, T.R.D. Architecture of the outer-membrane core complex from a conjugative type IV secretion system. Nat Commun, 12:6834-6834, 2021 Cited by PubMed Abstract: Conjugation is one of the most important processes that bacteria utilize to spread antibiotic resistance genes among bacterial populations. Interbacterial DNA transfer requires a large double membrane-spanning nanomachine called the type 4 secretion system (T4SS) made up of the inner-membrane complex (IMC), the outer-membrane core complex (OMCC) and the conjugative pilus. The iconic F plasmid-encoded T4SS has been central in understanding conjugation for several decades, however atomic details of its structure are not known. Here, we report the structure of a complete conjugative OMCC encoded by the pED208 plasmid from E. coli, solved by cryo-electron microscopy at 3.3 Å resolution. This 2.1 MDa complex has a unique arrangement with two radial concentric rings, each having a different symmetry eventually contributing to remarkable differences in protein stoichiometry and flexibility in comparison to other OMCCs. Our structure suggests that F-OMCC is a highly dynamic complex, with implications for pilus extension and retraction during conjugation. PubMed: 34824240DOI: 10.1038/s41467-021-27178-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.34 Å) |
Structure validation
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