Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II Journal Article
| Authors: | Fabrega, C.; Shen, V.; Shuman, S.; Lima, C. D. |
| Article Title: | Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II |
| Abstract: | The 2.7 Å structure of Candida albicans RNA guanylyltransferase Cgt1 cocrystallized with a carboxy-terminal domain (CTD) peptide composed of four Ser5-PO4 YSPTSPS heptad repeats illuminates distinct CTD-docking sites localized to the Cgt1 N-terminal nucleotidyl transferase domain. Tyr1, Pro3, Pro6, and Ser5-PO4 side chains from each of two YSPTSPS repeats contribute to the interface. Comparison to the Pin1-CTD structure shows that the CTD can assume markedly different conformations that are templated by particular binding partners. Structural plasticity combined with remodeling of CTD primary structure by kinases and phosphatases provides a versatile mechanism by which the CTD can recruit structurally dissimilar proteins during transcription. A binding site for the RNA triphosphatase component of the capping apparatus was also uncovered within the Cgt1 OB domain. |
| Keywords: | unclassified drug; mutation; sequence deletion; nonhuman; comparative study; protein domain; serine; carboxy terminal sequence; protein binding; enzyme activity; acid anhydride hydrolases; phosphorylation; enzyme phosphorylation; transcription regulation; amino acid sequence; molecular sequence data; sequence homology, amino acid; messenger rna; saccharomyces cerevisiae; rna caps; amino acid; models, molecular; crystallography, x-ray; protein structure, tertiary; binding sites; point mutation; enzyme binding; enzyme structure; phosphate; phosphotransferase; rna polymerase ii; enzyme localization; candida albicans; enzyme active site; enzyme conformation; nucleotidyltransferases; article; capping phenomenon; tyrosylserylprolylthreonylserylprolylserine |
| Journal Title: | Molecular Cell |
| Volume: | 11 |
| Issue: | 6 |
| ISSN: | 1097-2765 |
| Publisher: | Cell Press |
| Date Published: | 2003-06-01 |
| Start Page: | 1549 |
| End Page: | 1561 |
| Language: | English |
| DOI: | 10.1016/s1097-2765(03)00187-4 |
| PUBMED: | 12820968 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 12 September 2014 -- Source: Scopus |
