1d8h
From Proteopedia
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X-RAY CRYSTAL STRUCTURE OF YEAST RNA TRIPHOSPHATASE IN COMPLEX WITH SULFATE AND MANGANESE IONS.
Overview
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.
About this Structure
1D8H is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Polynucleotide 5'-phosphatase, with EC number 3.1.3.33 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:14:04 2008
Categories: Polynucleotide 5'-phosphatase | Saccharomyces cerevisiae | Single protein | Lima, C D. | Shuman, S. | Wang, L K. | MN | SO4 | Beta subunit | Catalytic domain | Dimer | Manganese/sulfate complex | Mrna capping | Mrna processing | Nuclear protein beta barrel | Polynucleotide 5'-triphosphatase | Rna triphosphatase
