- EMDB-13767: IMC-Arches-Stalk C1 at 6.18A - Refinement of the IMC, Arches and ... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-13767
タイトル
IMC-Arches-Stalk C1 at 6.18A - Refinement of the IMC, Arches and Stalk complex without symmetry from the fully-assembled R388 type IV secretion system.
マップデータ
IMC-Arches-Stalk C1 6.18A sharpened - Refinement of the Inner Membrane Complex (IMC), Arches and Stalk without symmetry.
試料
複合体: Type IV secretion system complex
タンパク質・ペプチド: TrwG protein
キーワード
type IV secretion system / type 4 secretion system / T4SS / IMC / inner membrane complex / inner membrane / arches / stalk / periplasmic / R388 plasmid / conjugation / bacterial secretion / secretion / secretion system / protein complex / VirB3 / VirB4 / VirB5 / VirB6 / VirB8 / TrwM / TrwK / TrwJ / TrwI / TrwG / MEMBRANE PROTEIN
機能・相同性
Type IV secretion system protein VirB8/PtlE / Bacterial virulence protein VirB8 / VirB8 protein / protein secretion by the type IV secretion system / NTF2-like domain superfamily / membrane / TrwG protein
ジャーナル: Nature / 年: 2022 タイトル: Cryo-EM structure of a type IV secretion system. 著者: Kévin Macé / Abhinav K Vadakkepat / Adam Redzej / Natalya Lukoyanova / Clasien Oomen / Nathalie Braun / Marta Ukleja / Fang Lu / Tiago R D Costa / Elena V Orlova / David Baker / Qian Cong / ...著者: Kévin Macé / Abhinav K Vadakkepat / Adam Redzej / Natalya Lukoyanova / Clasien Oomen / Nathalie Braun / Marta Ukleja / Fang Lu / Tiago R D Costa / Elena V Orlova / David Baker / Qian Cong / Gabriel Waksman / 要旨: Bacterial conjugation is the fundamental process of unidirectional transfer of DNAs, often plasmid DNAs, from a donor cell to a recipient cell. It is the primary means by which antibiotic resistance ...Bacterial conjugation is the fundamental process of unidirectional transfer of DNAs, often plasmid DNAs, from a donor cell to a recipient cell. It is the primary means by which antibiotic resistance genes spread among bacterial populations. In Gram-negative bacteria, conjugation is mediated by a large transport apparatus-the conjugative type IV secretion system (T4SS)-produced by the donor cell and embedded in both its outer and inner membranes. The T4SS also elaborates a long extracellular filament-the conjugative pilus-that is essential for DNA transfer. Here we present a high-resolution cryo-electron microscopy (cryo-EM) structure of a 2.8 megadalton T4SS complex composed of 92 polypeptides representing 8 of the 10 essential T4SS components involved in pilus biogenesis. We added the two remaining components to the structural model using co-evolution analysis of protein interfaces, to enable the reconstitution of the entire system including the pilus. This structure describes the exceptionally large protein-protein interaction network required to assemble the many components that constitute a T4SS and provides insights on the unique mechanism by which they elaborate pili.