9EKM

Thomasclavelia ramosa Immunoglobulin A Protease Middle (Protease) Domain with C-terminal Domain #1 (Metal Chelated)

9EKM の概要

• エントリーDOI: 10.2210/pdb9ekm/pdb
• 関連するPDBエントリー: 9EKK
• 分子名称: IgA protease, ZINC ION, PRASEODYMIUM ION, ... (4 entities in total)
• 機能のキーワード: m64 protease, secreted protein, immune modulating, zinc metalloprotease, hydrolase
• 由来する生物種: Thomasclavelia ramosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 125607.54

構造登録者

Tran, N.,Frenette, A.,Holyoak, T. (登録日: 2024-12-02, 公開日: 2025-09-03, 最終更新日: 2025-09-10)

主引用文献

Tran, N.,Frenette, A.,Holyoak, T.
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteases.
Proc.Natl.Acad.Sci.USA, 122:e2503549122-e2503549122, 2025

PubMed Abstract: Immunoglobulin A proteases (IgAPs) are a diverse group of enzymes secreted from bacteria that inhabit human mucosal tissues. These enzymes have convergently evolved to cleave human immunoglobulin A as a means of modulating and evading host immunity. Only two of three known IgAP families have been biochemically characterized beyond their initial discovery. Here, we show using solution-scattering, steady-state kinetic, and crystallographic approaches that the protease from , representing the uncharacterized third family, has a truly modular and minimizable protein architecture. This analysis also revealed a unique metal-associated domain that likely functions as a molecular spacer and generated a working hypothesis detailing the structural mechanism behind the enzyme's high substrate specificity. Our work provides an in-depth biochemical account of this IgAP family, paving the way for advancing clinically relevant IgAP-related research and our understanding of IgAPs as a whole.

PubMed: 40854123
DOI: 10.1073/pnas.2503549122

実験手法

X-RAY DIFFRACTION (1.5 Å)