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Structure of the Arabidopsis thaliana TOP2 oligopeptidase
- Publication Year :
- 2014
- Publisher :
- International Union of Crystallography, 2014.
-
Abstract
- Thimet oligopeptidase (TOP) is a zinc-dependent metallopeptidase. Recent studies suggest thatArabidopsis thalianaTOP1 and TOP2 are targets for salicylic acid (SA) binding and participate in SA-mediated plant innate immunity. The crystal structure ofA. thalianaTOP2 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 ofA. thalianaTOP1 and TOP2.
- Subjects :
- Metallopeptidase
Biophysics
Arabidopsis
Oligopeptidase
Biochemistry
Protein Structure, Secondary
chemistry.chemical_compound
X-Ray Diffraction
Structural Biology
Hydrolase
Genetics
Arabidopsis thaliana
Structural Communications
Humans
Amino Acid Sequence
Peptide sequence
Thimet oligopeptidase
biology
Arabidopsis Proteins
Metalloendopeptidases
Condensed Matter Physics
biology.organism_classification
chemistry
Salicylic acid
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....3b91bcc432a8c1a8c22e1c065b9432fa