3J6D

Model of the PrgH-PrgK periplasmic rings

3J6D の概要

• エントリーDOI: 10.2210/pdb3j6d/pdb
• 関連するPDBエントリー: 2MKY 4G1I 4OYC
• EMDBエントリー: 1875
• 分子名称: Protein PrgH, Pathogenicity 1 island effector protein (2 entities in total)
• 機能のキーワード: bacterial secression macromolecular assemblies, structural protein
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2; 詳細
• タンパク質・核酸の鎖数: 48
• 化学式量合計: 1746111.70

構造登録者

Bergeron, J.R.C.,Strynadka, N.C.J. (登録日: 2014-02-14, 公開日: 2015-01-14, 最終更新日: 2024-02-21)

主引用文献

Bergeron, J.R.,Worrall, L.J.,De, S.,Sgourakis, N.G.,Cheung, A.H.,Lameignere, E.,Okon, M.,Wasney, G.A.,Baker, D.,McIntosh, L.P.,Strynadka, N.C.
The Modular Structure of the Inner-Membrane Ring Component PrgK Facilitates Assembly of the Type III Secretion System Basal Body.
Structure, 23:161-172, 2015

PubMed Abstract: The type III secretion system (T3SS) is a large macromolecular assembly found at the surface of many pathogenic Gram-negative bacteria. Its role is to inject toxic "effector" proteins into the cells of infected organisms. The molecular details of the assembly of this large, multimembrane-spanning complex remain poorly understood. Here, we report structural, biochemical, and functional analyses of PrgK, an inner-membrane component of the prototypical Salmonella typhimurium T3SS. We have obtained the atomic structures of the two ring building globular domains and show that the C-terminal transmembrane helix is not essential for assembly and secretion. We also demonstrate that structural rearrangement of the two PrgK globular domains, driven by an interconnecting linker region, may promote oligomerization into ring structures. Finally, we used electron microscopy-guided symmetry modeling to propose a structural model for the intimately associated PrgH-PrgK ring interaction within the assembled basal body.

PubMed: 25533490
DOI: 10.1016/j.str.2014.10.021

実験手法

ELECTRON MICROSCOPY (11.7 Å)