2J9T

BipD of Burkholderia Pseudomallei

「2CMQ」から置き換えられました

2J9T の概要

• エントリーDOI: 10.2210/pdb2j9t/pdb
• 関連するPDBエントリー: 2IXR 2IZP
• 分子名称: MEMBRANE ANTIGEN, BORIC ACID, CITRATE ANION, ... (4 entities in total)
• 機能のキーワード: burkholderia pseudomallei, bipd, ttss, t3ss, type 3 secretion system, toxin
• 由来する生物種: BURKHOLDERIA PSEUDOMALLEI
• 細胞内の位置: Secreted : Q63K37
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66487.20

構造登録者

Johnson, S.,Roversi, P.,Field, T.,Deane, J.E.,Galyov, E.,Lea, S.M. (登録日: 2006-11-16, 公開日: 2006-11-20, 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-, 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 (2.7 Å)