Summary information and primary citation
- PDB-id
-
5bte;
DSSR-derived features in text and
JSON formats
- Class
- hydrolase-RNA
- Method
- X-ray (2.4 Å)
- Summary
- Crystal structure of ashbya gossypii rai1 in complex
with pu(s)6-mn2+
- Reference
-
Wang VY, Jiao X, Kiledjian M, Tong L (2015): "Structural
and biochemical studies of the distinct activity profiles
of Rai1 enzymes." Nucleic Acids Res.,
43, 6596-6606. doi: 10.1093/nar/gkv620.
- Abstract
- Recent studies showed that Rai1 and its homologs are a
crucial component of the mRNA 5'-end capping quality
control mechanism. They can possess RNA 5'-end
pyrophosphohydrolase (PPH), decapping, and 5'-3'
exonuclease (toward 5' monophosphate RNA) activities, which
help to degrade mRNAs with incomplete 5'-end capping. A
single active site in the enzyme supports these apparently
distinct activities. However, each Rai1 protein studied so
far has a unique set of activities, and the molecular basis
for these differences are not known. Here, we have
characterized the highly diverse activity profiles of Rai1
homologs from a collection of fungal organisms and
identified a new activity for these enzymes, 5'-end
triphosphonucleotide hydrolase (TPH) instead of PPH
activity. Crystal structures of two of these enzymes bound
to RNA oligonucleotides reveal differences in the RNA
binding modes. Structure-based mutations of these enzymes,
changing residues that contact the RNA but are poorly
conserved, have substantial effects on their activity,
providing a framework to begin to understand the molecular
basis for the different activity profiles.
