3DPN

Crystal Structure of cpaf s499a mutant

3DPN の概要

• エントリーDOI: 10.2210/pdb3dpn/pdb
• 関連するPDBエントリー: 3DJA 3DOR 3DPM
• 分子名称: Protein CT_858 (1 entity in total)
• 機能のキーワード: cpaf, s499a, zymogen, transferase
• 由来する生物種: Chlamydia trachomatis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 130757.66

構造登録者

Chai, J.,Huang, Z. (登録日: 2008-07-09, 公開日: 2009-01-13, 最終更新日: 2023-11-01)

主引用文献

Huang, Z.,Feng, Y.,Chen, D.,Wu, X.,Huang, S.,Wang, X.,Xiao, X.,Li, W.,Huang, N.,Gu, L.,Zhong, G.,Chai, J.
Structural basis for activation and inhibition of the secreted chlamydia protease CPAF
Cell Host Microbe, 4:529-542, 2008

PubMed Abstract: The obligate intracellular pathogen Chlamydia trachomatis is the most common cause of sexually transmitted bacterial disease. It secretes a protease known as chlamydial protease/proteasome-like activity factor (CPAF) that degrades many host molecules and plays a major role in Chlamydia pathogenesis. Here, we show that mature CPAF is a homodimer of the catalytic domains, each of which comprises two distinct subunits. Dormancy of the CPAF zymogen is maintained by an internal inhibitory segment that binds the CPAF active site and blocks its homodimerization. CPAF activation is initiated by trans-autocatalytic cleavage, which induces homodimerization and conformational changes that assemble the catalytic triad. This assembly leads to two autocatalytic cleavages and removal of the inhibitory segment, enabling full CPAF activity. CPAF is covalently bound and inhibited by the proteasome inhibitor lactacystin. These results reveal the activation mechanism of the CPAF serine protease and suggest new opportunities for anti-Chlamydia drug development.

PubMed: 19064254
DOI: 10.1016/j.chom.2008.10.005

実験手法

X-RAY DIFFRACTION (3.3 Å)