9BSH

Staphylococcus aureus exfoliative toxin A D164A variant

9BSH の概要

• エントリーDOI: 10.2210/pdb9bsh/pdb
• 分子名称: Exfoliative toxin A (2 entities in total)
• 機能のキーワード: exfoliative toxin, toxin
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62182.12

構造登録者

Holyoak, T.,Tran, N. (登録日: 2024-05-13, 公開日: 2025-04-23)

主引用文献

Lee, E.,Tran, N.,Redzic, J.S.,Singh, H.,Alamillo, L.,Holyoak, T.,Hamelberg, D.,Eisenmesser, E.Z.
Identifying and controlling inactive and active conformations of a serine protease.
Sci Adv, 11:eadu7447-eadu7447, 2025

PubMed Abstract: Serine proteases have been proposed to dynamically sample inactive and active conformations, but direct evidence at atomic resolution has remained elusive. Using nuclear magnetic resonance (NMR), we identified a single residue, D164, in exfoliative toxin A (ETA) that acts as a molecular "switch" to regulate global dynamic sampling. Mutations at this site shift the balance between inactive and active states, correlating directly with catalytic activity. Beyond identifying this dynamic switch, we demonstrate how it works in concert with other allosterically coupled sites to rationally control enzyme movements and catalytic function. This study provides a framework for linking conformational dynamics to function and paves the way for engineering enzymes, in particular, proteases, with tailored activities for applications in medicine and biotechnology.

PubMed: 40203097
DOI: 10.1126/sciadv.adu7447

実験手法

X-RAY DIFFRACTION (1.35 Å)