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Structure of a type IV secretion system core complex encoded by multi-drug resistance F plasmids.
- Source :
-
Nature communications [Nat Commun] 2022 Jan 19; Vol. 13 (1), pp. 379. Date of Electronic Publication: 2022 Jan 19. - Publication Year :
- 2022
-
Abstract
- Bacterial type IV secretion systems (T4SSs) are largely responsible for the proliferation of multi-drug resistance. We solved the structure of the outer-membrane core complex (OMCC <subscript>F</subscript> ) of a T4SS encoded by a conjugative F plasmid at <3.0 Å resolution by cryoelectron microscopy. The OMCC <subscript>F</subscript> consists of a 13-fold symmetrical outer ring complex (ORC) built from 26 copies of TraK and TraV C-terminal domains, and a 17-fold symmetrical central cone (CC) composed of 17 copies of TraB β-barrels. Domains of TraV and TraB also bind the CC and ORC substructures, establishing that these proteins undergo an intraprotein symmetry alteration to accommodate the C13:C17 symmetry mismatch. We present evidence that other pED208-encoded factors stabilize the C13:C17 architecture and define the importance of TraK, TraV and TraB domains to T4SS <subscript>F</subscript> function. This work identifies OMCC <subscript>F</subscript> structural motifs of proposed importance for structural transitions associated with F plasmid dissemination and F pilus biogenesis.<br /> (© 2022. The Author(s).)
Details
- Language :
- English
- ISSN :
- 2041-1723
- Volume :
- 13
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Nature communications
- Publication Type :
- Academic Journal
- Accession number :
- 35046412
- Full Text :
- https://doi.org/10.1038/s41467-022-28058-5