Molecular basis for cysteine oxidation by plant cysteine oxidases from Arabidopsis thaliana.
Cysteine oxidation
Mass spectrometry
Plant Cysteine Oxidase(s)
X-ray crystallography
Journal
Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206
Informations de publication
Date de publication:
03 2021
03 2021
Historique:
received:
14
10
2020
revised:
09
11
2020
accepted:
10
11
2020
pubmed:
19
11
2020
medline:
15
12
2021
entrez:
18
11
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33207269
pii: S1047-8477(20)30236-7
doi: 10.1016/j.jsb.2020.107663
pii:
doi:
Substances chimiques
Arabidopsis Proteins
0
Arginine
94ZLA3W45F
Cysteine Dioxygenase
EC 1.13.11.20
Cysteine
K848JZ4886
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
107663Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.