7DFT

Crystal structure of Xanthomonas oryzae ClpP

Summary for 7DFT

• Entry DOI: 10.2210/pdb7dft/pdb
• Descriptor: ATP-dependent Clp protease proteolytic subunit, CHLORIDE ION (3 entities in total)
• Functional Keywords: caseinolytic protease p, clp protease, hydrolase
• Biological source: Xanthomonas oryzae
• Total number of polymer chains: 7
• Total formula weight: 160024.40

Authors

Yang, C.-G.,Yang, T. (deposition date: 2020-11-09, release date: 2021-05-19, Last modification date: 2023-11-29)

Primary citation

Yang, T.,Zhang, T.,Zhou, X.,Wang, P.,Gan, J.,Song, B.,Yang, S.,Yang, C.G.
Dysregulation of ClpP by Small-Molecule Activators Used Against Xanthomonas oryzae pv. oryzae Infections.
J.Agric.Food Chem., 69:7545-7553, 2021

PubMed Abstract: Rice bacterial leaf blight caused by () is considered a destructive plant bacterial disease. The looming crisis of antibiotic resistance necessitates the discovery of antibiotics with new modes of action. Activated caseinolytic protease P (ClpP) can degrade bacterial FtsZ proteins that are essential for cell division; thus, we hypothesized that small-molecule-induced dysregulation of ClpP may result in degradation of FtsZ to treat leaf blight diseases. In this work, we have determined the crystal structures of ClpP, and its mutant bound with ADEP4, which revealed the action modes of ClpP assemblies and FtsZ degradation by dysregulated ClpP in the presence of small-molecule activators, such as ONC212 and ADEP4. Additionally, an antibacterial assessment demonstrated that ONC212 displays excellent activity against and prevents rice bacterial leaf blight . Thus, these unique antibacterial effects of small-molecule activators of ClpP represent a potential strategy for the development of agricultural antibiotics by targeting bacterial ClpP.

PubMed: 34218658
DOI: 10.1021/acs.jafc.1c01470

Experimental method

X-RAY DIFFRACTION (1.8 Å)