2BVB

The C-terminal domain from Micronemal Protein 1 (MIC1) from Toxoplasma Gondii

2BVB の概要

• エントリーDOI: 10.2210/pdb2bvb/pdb
• NMR情報: BMRB: 6376
• 分子名称: MICRONEMAL PROTEIN 1 (1 entity in total)
• 機能のキーワード: mic1, microneme, invasion, adhesion
• 由来する生物種: TOXOPLASMA GONDII
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle, microneme: O00834
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14030.57

構造登録者

Saouros, S.,Edwards-Jones, B.,Reiss, M.,Sawmynaden, K.,Cota, E.,Simpson, P.,Dowse, T.J.,Jakle, U.,Ramboarina, S.,Shivarattan, T.,Matthews, S.,Soldati-Favre, D. (登録日: 2005-06-23, 公開日: 2005-10-12, 最終更新日: 2024-11-06)

主引用文献

Saouros, S.,Edwards-Jones, B.,Reiss, M.,Sawmynaden, K.,Cota, E.,Simpson, P.,Dowse, T.J.,Jakle, U.,Ramboarina, S.,Shivarattan, T.,Matthews, S.,Soldati-Favre, D.
A Novel Galectin-Like Domain from Toxoplasma Gondll Micronemal Protein 1 Assists the Folding, Assembly,and Transport of a Cell-Adhesion Complex.
J.Biol.Chem., 280:38583-, 2005

PubMed Abstract: Immediately prior to invasion Toxoplasma gondii tachyzoites release a large number of micronemal proteins (TgMICs) that participate in host cell attachment and penetration. The TgMIC4-MIC1-MIC6 complex was the first to be identified in T. gondii and has been recently shown to be critical in invasion. This study establishes that the N-terminal thrombospondin type I repeat-like domains (TSR1-like) from TgMIC1 function as an independent adhesin as well as promoting association with TgMIC4. Using the newly solved three-dimensional structure of the C-terminal domain of TgMIC1 we have identified a novel Galectin-like fold that does not possess carbohydrate binding properties and redefines the architecture of TgMIC1. Instead, the TgMIC1 Galectin-like domain interacts and stabilizes TgMIC6, which provides the basis for a highly specific quality control mechanism for successful exit from the early secretory compartments and for subsequent trafficking of the complex to the micronemes.

PubMed: 16166092
DOI: 10.1074/JBC.C500365200

実験手法

SOLUTION NMR