- EMDB-12963: Structure of the outer-membrane core complex (outer ring) from a ... -
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基本情報
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データベース: EMDB / ID: EMD-12963
タイトル
Structure of the outer-membrane core complex (outer ring) from a conjugative type IV secretion system
マップデータ
The structure of the outer-membrane core complex (outer ring) from a conjugative type IV secretion system
試料
複合体: Outer-membrane core complex (outer ring)
タンパク質・ペプチド: Type IV conjugative transfer system lipoprotein TraV
タンパク質・ペプチド: TraB
タンパク質・ペプチド: Type-F conjugative transfer system secretin TraK
キーワード
Type IV secretion system / F plasmid / outer-membrane core complex / conjugation / MEMBRANE PROTEIN
機能・相同性
Pilus assembly TraK / Type-F conjugative transfer system secretin TraK / TraK protein / Type IV conjugative transfer system protein TraV / Type IV conjugative transfer system lipoprotein (TraV) / Prokaryotic membrane lipoprotein lipid attachment site profile. / Type-F conjugative transfer system secretin TraK / Type IV conjugative transfer system lipoprotein TraV
ジャーナル: Nat Commun / 年: 2021 タイトル: Architecture of the outer-membrane core complex from a conjugative type IV secretion system. 著者: Himani Amin / Aravindan Ilangovan / Tiago R D Costa / 要旨: 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 ...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.