2bf0

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2bf0, resolution 2.30Å

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CRYSTAL STRUCTURE OF THE RPR OF PCF11

Overview

The C-terminal domain (CTD) of the large subunit of RNA polymerase II is a platform for mRNA processing factors and links gene transcription to mRNA capping, splicing and polyadenylation. Pcf11, an essential component of the mRNA cleavage factor IA, contains a CTD-interaction domain that binds in a phospho-dependent manner to the heptad repeats within the RNA polymerase II CTD. We show here that the phosphorylated CTD exists as a dynamic disordered ensemble in solution and, by induced fit, it assumes a structured conformation when bound to Pcf11. In addition, we detected cis-trans populations for the CTD prolines, and found that only the all-trans form is selected for binding. These data suggest that the recognition of the CTD is regulated by independent site-specific modifications (phosphorylation and proline cis-trans isomerization) and, probably, by the local concentration of suitable binding sites.

About this Structure

2BF0 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Key features of the interaction between Pcf11 CID and RNA polymerase II CTD., Noble CG, Hollingworth D, Martin SR, Ennis-Adeniran V, Smerdon SJ, Kelly G, Taylor IA, Ramos A, Nat Struct Mol Biol. 2005 Feb;12(2):144-51. Epub 2005 Jan 16. PMID:15665873

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