5BUD
Crystal structure of Candida albicans Rai1 in complex with pU5-Mn2+
Summary for 5BUD
| Entry DOI | 10.2210/pdb5bud/pdb |
| Descriptor | Decapping nuclease RAI1, RNA (5'-R(P*UP*UP*UP*U)-3'), MANGANESE (II) ION, ... (4 entities in total) |
| Functional Keywords | rai1, rna, decapping, mrna 5'-processing, hydrolase-rna complex, hydrolase/rna |
| Biological source | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) More |
| Total number of polymer chains | 4 |
| Total formula weight | 95069.81 |
| Authors | Wang, V.Y.,Tong, L. (deposition date: 2015-06-03, release date: 2015-07-08, 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 Cited by 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: 26101253DOI: 10.1093/nar/gkv620 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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