Crystal structure of Arabidopsis thaliana cytidine deaminase release_rev_d97de6cf-fc8f-43f0-bd52-425b157c41ed

by Jia Wang, Qi Guo, Lin Liu, Xiao Wang

Published in Biochemical and Biophysical Research Communications - BBRC by Elsevier BV.

2020   Volume 529, Issue 3, p659-665

Abstract

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.
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Type  article-journal
Stage   published
Date   2020-07-18
Language   en ?
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ISSN-L:  0006-291X
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