2LV4

ZirS C-terminal Domain

2LV4 の概要

• エントリーDOI: 10.2210/pdb2lv4/pdb
• NMR情報: BMRB: 18553
• 分子名称: Putative outer membrane or exported protein (1 entity in total)
• 機能のキーワード: antivirulence, adhesion, protein binding
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16105.11

構造登録者

Prehna, G.,Li, Y.,Stoynov, N.,Okon, M.,Vukovic, M.,Mcintosh, L.P.,Foster, L.J.,Finlay, B.,Strynadka, N.C.J. (登録日: 2012-06-28, 公開日: 2012-08-22, 最終更新日: 2024-05-15)

主引用文献

Prehna, G.,Li, Y.,Stoynov, N.,Okon, M.,Vuckovic, M.,McIntosh, L.P.,Foster, L.J.,Finlay, B.B.,Strynadka, N.C.
The zinc regulated antivirulence pathway of salmonella is a multiprotein immunoglobulin adhesion system.
J.Biol.Chem., 287:32324-32337, 2012

PubMed Abstract: The co-evolutionary relationship between pathogen and host has led to a regulatory cycle between virulence factors needed for survival and antivirulence factors required for host transmission. This is exemplified in Salmonella spp. by the zirTS antivirulence genes: a secretion pathway comprised of the outer membrane transporter ZirT, and its secreted partner, ZirS. ZirTS act within the gastrointestinal tract to function as a virulence modulator and during Salmonella shedding in anticipation of a new host. Together, ZirT and ZirS decrease virulence by lowering bacterial colonization at systemic sites through an unknown mechanism. To understand this mechanism, we have probed the zirTS pathway both structurally and biochemically. The NMR derived structural ensemble of the C-terminal domain of ZirS reveals an immunoglobin superfamily fold (IgSF). Stable isotope labeling by amino acids in cell culture experiments show that the ZirS IgSF domain interacts with its transporter ZirT, and reveal a new protein interaction partner of the pathway, a protein encoded adjacent to zirTS that we have designated as ZirU. ZirU is secreted by ZirT and is also a predicted IgSF. Biochemical analysis delineates ZirT into an N-terminal porin-like β domain and C-terminal extracellular soluble IgSF domain, whereas biophysical characterization suggests that the transporter undergoes self-association in a concentration-dependent manner. We observe that ZirS and ZirU directly interact with each other and with the extracellular domains of ZirT. Here we show that the zir antivirulence pathway is a multiprotein immunoglobulin adhesion system consisting of a complex interplay between ZirS, ZirT, and ZirU.

PubMed: 22810234
DOI: 10.1074/jbc.M112.357210

実験手法

SOLUTION NMR