Structure and mechanism of yeast RNA triphosphatase: An essential component of the mRNA capping apparatus Journal Article
| Authors: | Lima, C. D.; Wang, L. K.; Shuman, S. |
| Article Title: | Structure and mechanism of yeast RNA triphosphatase: An essential component of the mRNA capping apparatus |
| Abstract: | RNA triphosphatase is an essential mRNA processing enzyme that catalyzes the first step in cap formation. The 2.05 Å crystal structure of yeast RNA triphosphatase Cet1p reveals a novel active site fold whereby an eight- stranded β barrel forms a topologically closed triphosphate tunnel. Interactions of a sulfate in the center of the tunnel with a divalent cation and basic amino acids projecting into the tunnel suggest a catalytic mechanism that is supported by mutational data. Discrete surface domains mediate Cet1p homodimerization and Cet1p binding to the guanylyltransferase component of the capping apparatus. The structure and mechanism of fungal RNA triphosphatases are completely different from those of mammalian mRNA capping enzymes. Hence, RNA triphosphatase presents an ideal target for structure- based antifungal drug discovery. |
| Keywords: | nonhuman; mammalia; phosphatase; protein binding; acid anhydride hydrolases; amino acid sequence; molecular sequence data; sequence homology, amino acid; messenger rna; saccharomyces cerevisiae; rna caps; computer simulation; models, molecular; dimerization; crystallography, x-ray; rna processing; enzyme structure; enzyme substrate complex; enzyme mechanism; rna processing, post-transcriptional; cations, divalent; rna capping; nucleotidyltransferases; priority journal; article |
| Journal Title: | Cell |
| Volume: | 99 |
| Issue: | 5 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 1999-11-24 |
| Start Page: | 533 |
| End Page: | 543 |
| Language: | English |
| PUBMED: | 10589681 |
| PROVIDER: | scopus |
| DOI: | 10.1016/S0092-8674(00)81541-X |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
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