2K2S

structure of the MIC1-GLD/MIC6-EGF complex from Toxoplasma gondii

2K2S の概要

• エントリーDOI: 10.2210/pdb2k2s/pdb
• 関連するPDBエントリー: 2K2T
• 分子名称: Micronemal protein 1, Micronemal protein 6 (2 entities in total)
• 機能のキーワード: microneme protein complex, cell adhesion, cytoplasmic vesicle, lectin, virulence, egf-like domain, membrane, transmembrane
• 由来する生物種: Toxoplasma gondii; 詳細
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle, microneme: O00834; Cytoplasmic vesicle, secretory vesicle, microneme membrane; Single-pass type I membrane protein: Q9XYH7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20325.55

構造登録者

Matthews, S. (登録日: 2008-04-11, 公開日: 2009-02-24, 最終更新日: 2024-10-16)

主引用文献

Sawmynaden, K.,Saouros, S.,Friedrich, N.,Marchant, J.,Simpson, P.,Bleijlevens, B.,Blackman, M.J.,Soldati-Favre, D.,Matthews, S.
Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition
Embo Rep., 9:1149-1155, 2008

PubMed Abstract: The obligate intracellular parasite Toxoplasma gondii, a member of the phylum Apicomplexa that includes Plasmodium spp., is one of the most widespread parasites and the causative agent of toxoplasmosis. Adhesive complexes composed of microneme proteins (MICs) are secreted onto the parasite surface from intracellular stores and fulfil crucial roles in host-cell recognition, attachment and penetration. Here, we report the high-resolution solution structure of a complex between two crucial MICs, TgMIC6 and TgMIC1. Furthermore, we identify two analogous interaction sites within separate epidermal growth factor-like (EGF) domains of TgMIC6-EGF2 and EGF3-and confirm that both interactions are functional for the recognition of host cell receptor in the parasite, using immunofluorescence and invasion assays. The nature of this new mode of recognition of the EGF domain and its abundance in apicomplexan surface proteins suggest a more generalized means of constructing functional assemblies by using EGF domains with highly specific receptor-binding properties.

PubMed: 18818666
DOI: 10.1038/embor.2008.179

実験手法

SOLUTION NMR