7VEP
Crystal structure and biophysical characterization of TPR domain of EccA5 from ESX-5 pathway of Mycobacterium tuberculosis H37RVR
Summary for 7VEP
| Entry DOI | 10.2210/pdb7vep/pdb |
| Descriptor | ESX-5 secretion system protein EccA5, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | ecca5, aaa+atpase, tpr domain, hydrolase |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Total number of polymer chains | 1 |
| Total formula weight | 31403.43 |
| Authors | Ramachandran, R.,Sharma, V.K.,Vishwakarma, J. (deposition date: 2021-09-09, release date: 2022-09-14, Last modification date: 2026-03-18) |
| Primary citation | 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 Cited by 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: 41761896DOI: 10.1002/1873-3468.70315 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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