2LO6

Structure of Nrd1 CID bound to phosphorylated RNAP II CTD

Summary for 2LO6

• Entry DOI: 10.2210/pdb2lo6/pdb
• NMR Information: BMRB: 17173
• Descriptor: Protein NRD1, DNA-directed RNA polymerase II subunit RPB1 (2 entities in total)
• Functional Keywords: ctd-interacting domain, cid, carboxy-terminal domain, ctd, rna-processing, transciption termination, cis-trans isomerization of prolines, ess1 isomerase, peptide binding protein, transcription
• Biological source: Saccharomyces cerevisiae S288c (Baker's yeast); More
• Cellular location: Nucleus (Potential): P53617; Nucleus: P04050
• Total number of polymer chains: 2
• Total formula weight: 19933.13

Authors

Kubicek, K.,Cerna, H.,Pasulka, J.,Holub, P.,Hrossova, D.,Loehr, F.,Hofr, C.,Vanacova, S.,Stefl, R. (deposition date: 2012-01-17, release date: 2012-12-26, Last modification date: 2024-11-06)

Primary citation

Kubicek, K.,Cerna, H.,Holub, P.,Pasulka, J.,Hrossova, D.,Loehr, F.,Hofr, C.,Vanacova, S.,Stefl, R.
Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1.
Genes Dev., 26:1891-1896, 2012

PubMed Abstract: Recruitment of appropriate RNA processing factors to the site of transcription is controlled by post-translational modifications of the C-terminal domain (CTD) of RNA polymerase II (RNAP II). Here, we report the solution structure of the Ser5 phosphorylated (pSer5) CTD bound to Nrd1. The structure reveals a direct recognition of pSer5 by Nrd1 that requires the cis conformation of the upstream pSer5-Pro6 peptidyl-prolyl bond of the CTD. Mutations at the complex interface diminish binding affinity and impair processing or degradation of noncoding RNAs. These findings underpin the interplay between covalent and noncovalent changes in the CTD structure that constitute the CTD code.

PubMed: 22892239
DOI: 10.1101/gad.192781.112

Experimental method

SOLUTION NMR