Summary information and primary citation
- PDB-id
-
6ozf;
DSSR-derived features in text and
JSON formats
- Class
- hydrolase
- Method
- X-ray (1.8 Å)
- Summary
- Crystal structure of thermotoga maritima (tm)
endonuclease v (d110n) in complex with a 12mer DNA
containing an inosine followed by a ribo-adenosine
- Reference
-
Wu J, Samara NL, Kuraoka I, Yang W (2019): "Evolution
of Inosine-Specific Endonuclease V from Bacterial DNase
to Eukaryotic RNase." Mol.Cell,
76, 44. doi: 10.1016/j.molcel.2019.06.046.
- Abstract
- Endonuclease V (EndoV) cleaves the second
phosphodiester bond 3' to a deaminated adenosine (inosine).
Although highly conserved, EndoV homologs change substrate
preference from DNA in bacteria to RNA in eukaryotes. We
have characterized EndoV from six different species and
determined crystal structures of human EndoV and three
EndoV homologs from bacteria to mouse in complex with
inosine-containing DNA/RNA hybrid or double-stranded RNA
(dsRNA). Inosine recognition is conserved, but changes in
several connecting loops in eukaryotic EndoV confer
recognition of 3 ribonucleotides upstream and 7 or
8 bp of dsRNA downstream of the cleavage site, and
bacterial EndoV binds only 2 or 3 nt flanking the scissile
phosphate. In addition to the two canonical metal ions in
the active site, a third Mn<sub>2+</sub> that
coordinates the nucleophilic water appears necessary for
product formation. Comparison of EndoV with its homologs
RNase H1 and Argonaute reveals the principles by which
these enzymes recognize RNA versus DNA.