Structural highlights
Function
[CET1_YEAST] First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
RNA triphosphatase is an essential mRNA processing enzyme that catalyzes the first step in cap formation. The 2.05 A crystal structure of yeast RNA triphosphatase Cet1p reveals a novel active site fold whereby an eight-stranded beta 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.
Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus.,Lima CD, Wang LK, Shuman S Cell. 1999 Nov 24;99(5):533-43. PMID:10589681[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hausmann S, Pei Y, Shuman S. Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases. J Biol Chem. 2003 Aug 15;278(33):30487-96. Epub 2003 Jun 3. PMID:12788946 doi:http://dx.doi.org/10.1074/jbc.M303060200
- ↑ Lima CD, Wang LK, Shuman S. Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus. Cell. 1999 Nov 24;99(5):533-43. PMID:10589681
