1P16
Structure of an mRNA capping enzyme bound to the phosphorylated carboxyl-terminal domain of RNA polymerase II
Summary for 1P16
| Entry DOI | 10.2210/pdb1p16/pdb |
| Descriptor | mRNA capping enzyme alpha subunit, phosphorylated peptide from C-terminal of RNA polymerase II, PHOSPHATE ION, ... (6 entities in total) |
| Functional Keywords | guanylyltransferase, candida albicans, rna polymerase ii, transcription, capping, ctd, mrna, transferase |
| Biological source | Candida albicans More |
| Cellular location | Nucleus: P78587 |
| Total number of polymer chains | 4 |
| Total formula weight | 98998.98 |
| Authors | Fabrega, C.,Shen, V.,Shuman, S.,Lima, C.D. (deposition date: 2003-04-11, release date: 2003-07-15, Last modification date: 2024-10-16) |
| Primary citation | Fabrega, C.,Shen, V.,Shuman, S.,Lima, C.D. Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II. Mol.Cell, 11:1549-1561, 2003 Cited by PubMed Abstract: The 2.7 A 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. PubMed: 12820968DOI: 10.1016/S1097-2765(03)00187-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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