7cxz | pdb_00007cxz
crystal structure of pco2
Structural highlights
Function[PCO2_ARATH] Oxidizes N-terminal cysteine residues, thus preparing the protein for N-end rule pathway-mediated proteasomal degradation. Controls the preparation of ERF-VII proteins for degradation via the 26S proteasome. Not active on Cys located inside or at the C-terminus of a peptide. Represses the anaerobic response.[1] Publication Abstract from PubMedPlant Cysteine Oxidases (PCOs) play important roles in controlling the stability of Group VII ethylene response factors (ERF-VIIs) via Arg/N-degron pathway through catalyzing the oxidation of their N-Cys for subsequent Arginyl-tRNA--protein transferase 1 (ATE1) mediated arginine installation. Here we presented the crystal structures of PCO2, PCO4, and PCO5 from Arabidopsis thaliana (AtPCOs) and examined their in vitro activity by Mass spectrometry (MS). On the basis of Tris-bound AtPCO2, we modelled the structure of Cys-bound AtPCO2 and identified key AtPCO2 residues involved in N-Cys recognition and oxidation. Alanine substitution of potential N-Cys interaction residues impaired the activity of AtPCO5 remarkably. The structural research, complemented by mutagenesis and MS experiments, not only uncovers the substrate recognition and catalytic mode by AtPCOs, but also sheds light on the future design of potent inhibitors for plant cysteine oxidases. Molecular basis for cysteine oxidation by plant cysteine oxidases from Arabidopsis thaliana.,Chen Z, Guo Q, Wu G, Wen J, Liao S, Xu C J Struct Biol. 2021 Mar;213(1):107663. doi: 10.1016/j.jsb.2020.107663. Epub 2020 , Nov 15. PMID:33207269[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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