5TCP

Near-atomic resolution cryo-EM structure of the periplasmic domains of PrgH and PrgK

5TCP の概要

• エントリーDOI: 10.2210/pdb5tcp/pdb
• 関連するPDBエントリー: 5TCQ 5TCR
• EMDBエントリー: 8398 8399 8400 8401
• 分子名称: Lipoprotein PrgK, Protein PrgH (2 entities in total)
• 機能のキーワード: bacterial, secretion, injectisome, membrane protein
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium; 詳細
• タンパク質・核酸の鎖数: 48
• 化学式量合計: 1357446.24

構造登録者

Worrall, L.J.,Hong, C.,Vuckovic, M.,Bergeron, J.R.C.,Huang, R.K.,Yu, Z.,Strynadka, N.C.J. (登録日: 2016-09-15, 公開日: 2016-12-21, 最終更新日: 2024-03-13)

主引用文献

Worrall, L.J.,Hong, C.,Vuckovic, M.,Deng, W.,Bergeron, J.R.,Majewski, D.D.,Huang, R.K.,Spreter, T.,Finlay, B.B.,Yu, Z.,Strynadka, N.C.
Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body.
Nature, 540:597-601, 2016

PubMed Abstract: The type III secretion (T3S) injectisome is a specialized protein nanomachine that is critical for the pathogenicity of many Gram-negative bacteria, including purveyors of plague, typhoid fever, whooping cough, sexually transmitted infections and major nosocomial infections. This syringe-shaped 3.5-MDa macromolecular assembly spans both bacterial membranes and that of the infected host cell. The internal channel formed by the injectisome allows for the direct delivery of partially unfolded virulence effectors into the host cytoplasm. The structural foundation of the injectisome is the basal body, a molecular lock-nut structure composed predominantly of three proteins that form highly oligomerized concentric rings spanning the inner and outer membranes. Here we present the structure of the prototypical Salmonella enterica serovar Typhimurium pathogenicity island 1 basal body, determined using single-particle cryo-electron microscopy, with the inner-membrane-ring and outer-membrane-ring oligomers defined at 4.3 Å and 3.6 Å resolution, respectively. This work presents the first, to our knowledge, high-resolution structural characterization of the major components of the basal body in the assembled state, including that of the widespread class of outer-membrane portals known as secretins.

PubMed: 27974800
DOI: 10.1038/nature20576

実験手法

ELECTRON MICROSCOPY (4.3 Å)