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 CA 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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