8JQZ

Crystal Structure of GppNHp-bound mIRGB10

8JQZ の概要

• エントリーDOI: 10.2210/pdb8jqz/pdb
• 分子名称: Immunity-related GTPase family member b10, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER (2 entities in total)
• 機能のキーワード: gtp hydrolase, immune system
• 由来する生物種: Mus musculus molossinus (Japanese wild mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95283.60

構造登録者

Ha, H.J.,Park, H.H. (登録日: 2023-06-15, 公開日: 2024-04-24)

主引用文献

Ha, H.J.,Kim, J.H.,Lee, G.H.,Kim, S.,Park, H.H.
Structural basis of IRGB10 oligomerization by GTP hydrolysis.
Front Immunol, 14:1254415-1254415, 2023

PubMed Abstract: Immunity-related GTPase B10 (IRGB10) is a crucial member of the interferon (IFN)-inducible GTPases and plays a vital role in host defense mechanisms. Following infection, IRGB10 is induced by IFNs and functions by liberating pathogenic ligands to activate the inflammasome through direct disruption of the pathogen membrane. Despite extensive investigation into the significance of the cell-autonomous immune response, the precise molecular mechanism underlying IRGB10-mediated microbial membrane disruption remains elusive. Herein, we present two structures of different forms of IRGB10, the nucleotide-free and GppNHp-bound forms. Based on these structures, we identified that IRGB10 exists as a monomer in nucleotide-free and GTP binding states. Additionally, we identified that GTP hydrolysis is critical for dimer formation and further oligomerization of IRGB10. Building upon these observations, we propose a mechanistic model to elucidate the working mechanism of IRGB10 during pathogen membrane disruption.

PubMed: 37705969
DOI: 10.3389/fimmu.2023.1254415

実験手法

X-RAY DIFFRACTION (3.05 Å)