1994
DOI: 10.1006/jmbi.1994.1018
|View full text |Cite
|
Sign up to set email alerts
|

Cytidine Deaminase. The 2·3 Å Crystal Structure of an Enzyme: Transition-state Analog Complex

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

16
424
0

Year Published

1997
1997
2011
2011

Publication Types

Select...
6
3

Relationship

0
9

Authors

Journals

citations
Cited by 369 publications
(442 citation statements)
references
References 0 publications
16
424
0
Order By: Relevance
“…The three dimensional structure of APOBEC3G has not yet been determined; however, the crystal structure of E. coli cytidine deaminase has been solved to high resolution (29). Although only distantly related in primary sequence, the enzyme has features that suggest conservation of structure.…”
Section: Discussionmentioning
confidence: 99%
“…The three dimensional structure of APOBEC3G has not yet been determined; however, the crystal structure of E. coli cytidine deaminase has been solved to high resolution (29). Although only distantly related in primary sequence, the enzyme has features that suggest conservation of structure.…”
Section: Discussionmentioning
confidence: 99%
“…The predicted dADAR protein is approximately the same size as the mammalian ADAR2 homologs (dADAR ϭ 670 amino acids, ratADAR2 ϭ 711 amino acids, ratRED2 ϭ 746 amino acids)+ Overall, dADAR has 43% identity to rADAR2 and 35% identity to RED2+ Within the deaminase domain, however, the homology rises to 46% identity for hADAR1 and 67% identity for hADAR2 enzymes+ Residues important for coordinating zinc in the catalytic domain are also absolutely conserved (Betts et al+, 1994;Kim et al+, 1994, Lai et al+, 1995 (Fig+ 3)+ In contrast, comparison with a tRNA-specific adenosine deaminase, dADAT1, revealed only 17% identity overall and 28% identity within the catalytic domain (Keegan et al+, 1999)+ dADAR encodes a dsRNA-specific adenosine deaminase…”
Section: Cdna Analysis Of Dadarmentioning
confidence: 99%
“…We discovered a nucleotide position in the dADAR transcript in exon 7 (Fig+ 1) that gave a reproducible mixed A/G signal in automated sequencing of bulk dADAR RT-PCR product (Fig+ 7A)+ Cloning and sequencing of dADAR transcripts showed that cDNAs also contained either A or G at the same position+ Because inosine base pairs preferentially with cytosine, an A-to-G transition occurs in the course of synthesis of doublestranded cDNA when A-to-I editing occurs in pre-mRNA+ Sequencing of PCR products generated from genomic DNA gave exclusively an A signal at the same position+ Also, P1 bacteriophage genomic clones containing the dADAR locus had A at this position+ Similar analyses were performed on genomic DNAs and RT-PCR products of related Drosophila species (Fig+ 7B)+ D. simulans is estimated to be 2+5 million years diverged from D. melanogaster (Powell, 1997)+ In each case, RT-PCR products revealed a mixed A/G signal at the same location in the related species whereas sequence of the corresponding PCR products generated from genomic DNA gave a pure A signal+ Thus, the A-to-G changes seen in cDNAs of dADAR, at variance with the genomically encoded A at this position, bear all the hallmarks of ADAR mediated A-to-I RNA editing seen in other natural mRNA substrates+ The A that is edited occurs in the first position of a serine (S) codon and would convert the coding potential to that of glycine (G) (AGT to GGT)+ This amino acid change occurs in the deaminase domain of dADAR, which is a highly conserved portion of the dADAR protein+ The S/G site is six amino acids carboxy-terminal to the first cysteine in motif II of the deaminase domain that is thought to chelate a zinc ion at the active site (Betts et al+, 1994;Kim et al+, 1994;Lai et al+, 1995) …”
Section: Dadar Itself Undergoes Rna Editingmentioning
confidence: 99%
“…Deaminases are also responsible for free nucleotide interconversions that contribute to nucleotide pools in cells and serve as a repository for the nucleotide building blocks used in both RNA and DNA synthesis (Wolfenden 1993;Betts et al 1994). In addition, deamination reactions have key functions in various metabolic pathways, for example, in riboflavin biosynthesis and threonine catabolism (Chen et al 2006;Simanshu et al 2006).…”
Section: Introductionmentioning
confidence: 99%