3J9G

Atomic model of the VipA/VipB, the type six secretion system contractile sheath of Vibrio cholerae from cryo-EM

これはPDB形式変換不可エントリーです。

3J9G の概要

• エントリーDOI: 10.2210/pdb3j9g/pdb
• EMDBエントリー: 2699
• 分子名称: VipA, VipB (2 entities in total)
• 機能のキーワード: t6ss, bacterial secretion, phage, contraction, contractile protein
• 由来する生物種: Vibrio cholerae O1 biovar El Tor str. N16961; 詳細
• タンパク質・核酸の鎖数: 60
• 化学式量合計: 1886523.00

構造登録者

Kudryashev, M.,Wang, R.Y.-R.,Brackmann, M.,Scherer, S.,Maier, T.,Baker, D.,DiMaio, F.,Stahlberg, H.,Egelman, E.H.,Basler, M. (登録日: 2015-01-16, 公開日: 2015-03-11, 最終更新日: 2024-02-21)

主引用文献

Kudryashev, M.,Wang, R.Y.,Brackmann, M.,Scherer, S.,Maier, T.,Baker, D.,DiMaio, F.,Stahlberg, H.,Egelman, E.H.,Basler, M.
Structure of the Type VI Secretion System Contractile Sheath.
Cell(Cambridge,Mass.), 160:952-962, 2015

PubMed Abstract: Bacteria use rapid contraction of a long sheath of the type VI secretion system (T6SS) to deliver effectors into a target cell. Here, we present an atomic-resolution structure of a native contracted Vibrio cholerae sheath determined by cryo-electron microscopy. The sheath subunits, composed of tightly interacting proteins VipA and VipB, assemble into a six-start helix. The helix is stabilized by a core domain assembled from four β strands donated by one VipA and two VipB molecules. The fold of inner and middle layers is conserved between T6SS and phage sheaths. However, the structure of the outer layer is distinct and suggests a mechanism of interaction of the bacterial sheath with an accessory ATPase, ClpV, that facilitates multiple rounds of effector delivery. Our results provide a mechanistic insight into assembly of contractile nanomachines that bacteria and phages use to translocate macromolecules across membranes.

PubMed: 25723169
DOI: 10.1016/j.cell.2015.01.037

実験手法

ELECTRON MICROSCOPY (3.5 Å)