7VEP

Crystal structure and biophysical characterization of TPR domain of EccA5 from ESX-5 pathway of Mycobacterium tuberculosis H37RVR

7VEP の概要

• エントリーDOI: 10.2210/pdb7vep/pdb
• 分子名称: ESX-5 secretion system protein EccA5, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: ecca5, aaa+atpase, tpr domain, hydrolase
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31403.43

構造登録者

Ramachandran, R.,Sharma, V.K.,Vishwakarma, J. (登録日: 2021-09-09, 公開日: 2022-09-14, 最終更新日: 2026-03-18)

主引用文献

Sharma, V.K.,Vishwakarma, J.,Kabrambam, R.,Kumar, S.,Ramachandran, R.
The crystal structure of the TPR domain of the EccA5 ATPase and demonstration of its interaction with EspG5 from the mycobacterial ESX-5 pathway.
Febs Lett., 2026

PubMed Abstract: The ESX-5 secretion system in Mycobacterium tuberculosis exports PE/PPE virulence factors, with EccA5, an AAA+ ATPase, playing a pivotal role. We solved the crystal structure of EccA5's N-terminal TPR domain (EccA5NT) at 2.15 Å, revealing a monomeric fold with six TPR motifs and a variable β-finger. Biophysical studies, including SAXS and size exclusion chromatography, confirm its monomeric state. A flexible loop (residues 137-148) suggests dynamic substrate interactions. SPR, SAXS and in silico docking show moderate binding (K = 3.43 μm) between EccA5NT's β-finger and EspG5's β2-β3 loop, indicating a role in PE/PPE-EspG5 complex disassembly. These findings elucidate the role of EccA5 in ESX-5-mediated secretion.

PubMed: 41761896
DOI: 10.1002/1873-3468.70315

実験手法

X-RAY DIFFRACTION (2.15 Å)