5BTE

Crystal structure of Ashbya gossypii Rai1 in complex with pU(S)6-Mn2+

Summary for 5BTE

• Entry DOI: 10.2210/pdb5bte/pdb
• Related: 5BTB 5BTH 5BTO
• Descriptor: AFR263Cp, RNA (5'-R(P*UP*(U37)P*(U37)P*UP*UP*U)-3'), MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: rai1, rna, decapping, mrna 5'-processing, hydrolase-rna complex, hydrolase/rna
• Biological source: Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast); More
• Total number of polymer chains: 4
• Total formula weight: 90394.47

Authors

Wang, V.Y.,Tong, L. (deposition date: 2015-06-03, release date: 2015-07-22, Last modification date: 2024-03-06)

Primary citation

Wang, V.Y.,Jiao, X.,Kiledjian, M.,Tong, L.
Structural and biochemical studies of the distinct activity profiles of Rai1 enzymes.
Nucleic Acids Res., 43:6596-6606, 2015

PubMed 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.

PubMed: 26101253
DOI: 10.1093/nar/gkv620

Experimental method

X-RAY DIFFRACTION (2.4 Å)