2BF0

crystal structure of the rpr of pcf11

Summary for 2BF0

• Entry DOI: 10.2210/pdb2bf0/pdb
• Related: 1SZ9 1SZA
• Descriptor: PCF11, CALCIUM ION (3 entities in total)
• Functional Keywords: transcription, rna, phosphorylation
• Biological source: SACCHAROMYCES CEREVISIAE (BAKERS YEAST)
• Cellular location: Nucleus (Potential): P39081
• Total number of polymer chains: 1
• Total formula weight: 16673.78

Authors

Noble, C.G.,Hollingworth, D.,Martin, S.R.,Adeniran, V.E.,Smerdon, S.J.,Kelly, G.,Taylor, I.A.,Ramos, A. (deposition date: 2004-12-02, release date: 2005-01-18, Last modification date: 2024-11-06)

Primary citation

Noble, C.G.,Hollingworth, D.,Martin, S.R.,Adeniran, V.E.,Smerdon, S.J.,Kelly, G.,Taylor, I.A.,Ramos, A.
Key Features of the Interaction between Pcf11 Cid and RNA Polymerase II Ctd.
Nat.Struct.Mol.Biol., 12:144-, 2005

PubMed Abstract: 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.

PubMed: 15665873
DOI: 10.1038/NSMB887

Experimental method

X-RAY DIFFRACTION (2.3 Å)