2J0O

Shigella Flexneri IpaD

2J0O の概要

• エントリーDOI: 10.2210/pdb2j0o/pdb
• 関連するPDBエントリー: 2J0N
• 分子名称: INVASIN IPAD, GLYCEROL (3 entities in total)
• 機能のキーワード: shigella flexneri, type iii secretion, cell invasion, ipad, t3ss, plasmid, invasin, virulence
• 由来する生物種: Shigella flexneri 2a str. 301
• 細胞内の位置: Secreted : P18013
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70588.56

構造登録者

Johnson, S.,Roversi, P.,Lea, S.M. (登録日: 2006-08-04, 公開日: 2006-11-02, 最終更新日: 2024-05-08)

主引用文献

Johnson, S.,Roversi, P.,Espina, M.,Olive, A.,Deane, J.E.,Birket, S.,Field, T.,Picking, W.D.,Blocker, A.J.,Galyov, E.E.,Picking, W.L.,Lea, S.M.
Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.
J. Biol. Chem., 282:4035-4044, 2007

PubMed Abstract: Bacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. The T3SS is composed of a basal body, which traverses both bacterial membranes, and an external needle through which effector proteins are secreted. We report multiple crystal structures of two proteins that sit at the tip of the needle and are essential for virulence: IpaD from Shigella flexneri and BipD from Burkholderia pseudomallei. The structures reveal that the N-terminal domains of the molecules are intramolecular chaperones that prevent premature oligomerization, as well as sharing structural homology with proteins involved in eukaryotic actin rearrangement. Crystal packing has allowed us to construct a model for the tip complex that is supported by mutations designed using the structure.

PubMed: 17077085
DOI: 10.1074/jbc.M607945200

実験手法

X-RAY DIFFRACTION (3 Å)