Crystal structure of Arabidopsis thaliana cytidine deaminase.
Catalytic mechanism
Crystallography
Pyrimidine metabolism
RNA editing
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
27 08 2020
27 08 2020
Historique:
received:
17
06
2020
accepted:
17
06
2020
entrez:
2
8
2020
pubmed:
2
8
2020
medline:
13
2
2021
Statut:
ppublish
Résumé
Cytidine deaminase (CDA) catalyzes the (deoxy)cytidine deamination to (deoxy)uridine, which involves in the catabolic and salvage pathways of pyrimidine nucleotides in plants. CDA serves as a prototype of the cytidine deaminase superfamily that contains a number of RNA editing enzymes. Arabidopsis thaliana has only one functional CDA, AtCDA1. We solved the crystal structures of AtCDA1, which is a dimeric zinc-containing enzyme and each protomer consists of an N-terminal zinc-binding catalytic domain and a C-terminal non-catalytic domain. Both domains adopt a typical α/β/α sandwich fold. In vitro biochemical assays showed that the ribose moiety of cytidine is required for ligand binding, and structural analyses revealed a conserved catalytic mechanism is adopted by AtCDA1.
Identifiants
pubmed: 32736689
pii: S0006-291X(20)31302-4
doi: 10.1016/j.bbrc.2020.06.084
pii:
doi:
Substances chimiques
Arabidopsis Proteins
0
Cytidine Deaminase
EC 3.5.4.5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
659-665Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.