2LO6

Structure of Nrd1 CID bound to phosphorylated RNAP II CTD

2LO6 の概要

• エントリーDOI: 10.2210/pdb2lo6/pdb
• NMR情報: BMRB: 17173
• 分子名称: Protein NRD1, DNA-directed RNA polymerase II subunit RPB1 (2 entities in total)
• 機能のキーワード: ctd-interacting domain, cid, carboxy-terminal domain, ctd, rna-processing, transciption termination, cis-trans isomerization of prolines, ess1 isomerase, peptide binding protein, transcription
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast); 詳細
• 細胞内の位置: Nucleus (Potential): P53617; Nucleus: P04050
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19933.13

構造登録者

Kubicek, K.,Cerna, H.,Pasulka, J.,Holub, P.,Hrossova, D.,Loehr, F.,Hofr, C.,Vanacova, S.,Stefl, R. (登録日: 2012-01-17, 公開日: 2012-12-26)

主引用文献

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

実験手法

SOLUTION NMR