4PUT

Crystal structure of the Arabidopsis thaliana TOP2 oligopeptidase

Summary for 4PUT

• Entry DOI: 10.2210/pdb4put/pdb
• Descriptor: Cytosolic oligopeptidase A, ZINC ION, CHLORIDE ION (3 entities in total)
• Functional Keywords: oligopeptidase, hydrolase
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Cytoplasm, cytosol: Q949P2
• Total number of polymer chains: 1
• Total formula weight: 81417.06

Authors

Wang, R.,Rajagopalan, K.,Tong, L. (deposition date: 2014-03-13, release date: 2014-05-14, Last modification date: 2024-02-28)

Primary citation

Wang, R.,Rajagopalan, K.,Sadre-Bazzaz, K.,Moreau, M.,Klessig, D.F.,Tong, L.
Structure of the Arabidopsis thaliana TOP2 oligopeptidase.
Acta Crystallogr F Struct Biol Commun, 70:555-559, 2014

PubMed Abstract: Thimet oligopeptidase (TOP) is a zinc-dependent metallopeptidase. Recent studies suggest that Arabidopsis thaliana TOP1 and TOP2 are targets for salicylic acid (SA) binding and participate in SA-mediated plant innate immunity. The crystal structure of A. thaliana TOP2 has been determined at 3.0 Å resolution. Comparisons to the structure of human TOP revealed good overall structural conservation, especially in the active-site region, despite their weak sequence conservation. The protein sample was incubated with the photo-activated SA analog 4-azido-SA and exposed to UV irradiation before crystallization. However, there was no conclusive evidence for the binding of SA based on the X-ray diffraction data. Further studies are needed to elucidate the molecular mechanism of how SA regulates the activity of A. thaliana TOP1 and TOP2.

PubMed: 24817709
DOI: 10.1107/S2053230X14006128

Experimental method

X-RAY DIFFRACTION (3 Å)