Structure of a type IV secretion system core complex encoded by multi-drug resistance F plasmids.

Structure of a type IV secretion system core complex encoded by multi-drug resistance F plasmids.
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DOI:
10.1038/s41467-022-28058-5
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发表时间:
2022-01-19
影响因子:
16.6
通讯作者:
Hu B
Hu B
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Liu X;Khara P;Baker ML;Christie PJ;Hu B

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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 (OMCCF) of a T4SS encoded by a conjugative F plasmid at <3.0 Å resolution by cryoelectron microscopy. The OMCCF 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 T4SSF function. This work identifies OMCCF structural motifs of proposed importance for structural transitions associated with F plasmid dissemination and F pilus biogenesis. Bacteria conjugatively transfer DNA through type IV secretion systems (T4SSs). Here, the authors report the structure of a T4SS outer-membrane core complex (OMCC), revealing how a distinct C13:C17 symmetry mismatch exhibited by peripheral ring and central cone substructures is accommodated.
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发表时间: 2018-07-01
期刊: EcoSal Plus
影响因子: --
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