1p16

From Proteopedia

Revision as of 21:15, 20 November 2007

Structure of an mRNA capping enzyme bound to the phosphorylated carboxyl-terminal domain of RNA polymerase II

Overview

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.

About this Structure

1P16 is a Single protein structure of sequence from Candida albicans with PO4, G and GTP as ligands. Active as mRNA guanylyltransferase, with EC number 2.7.7.50 Full crystallographic information is available from OCA.

Reference

Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II., Fabrega C, Shen V, Shuman S, Lima CD, Mol Cell. 2003 Jun;11(6):1549-61. PMID:12820968

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