7CHI

crystal structure of pco5

Summary for 7CHI

• Entry DOI: 10.2210/pdb7chi/pdb
• Descriptor: Plant cysteine oxidase 5, FE (III) ION (3 entities in total)
• Functional Keywords: oxidase, metal binding, enzyme, metal binding protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 27834.42

Authors

Guo, Q.,Xu, C.,Liao, S. (deposition date: 2020-07-05, release date: 2020-11-25, Last modification date: 2021-03-31)

Primary citation

Chen, Z.,Guo, Q.,Wu, G.,Wen, J.,Liao, S.,Xu, C.
Molecular basis for cysteine oxidation by plant cysteine oxidases from Arabidopsis thaliana.
J.Struct.Biol., 213:107663-107663, 2021

PubMed Abstract: Plant 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.

PubMed: 33207269
DOI: 10.1016/j.jsb.2020.107663

Experimental method

X-RAY DIFFRACTION (2.502 Å)