PDBsum entry 2lo6

Transcription

PDB id: 2lo6

Contents

Protein chains

154 a.a.

14 a.a.

PDB id:

2lo6

Name:

Transcription

Title:

Structure of nrd1 cid bound to phosphorylated rnap ii ctd

Structure:

Protein nrd1. Chain: a. Fragment: cid domain residues 1-154. Engineered: yes. DNA-directed RNA polymerase ii subunit rpb1. Chain: b. Fragment: unp residues 1556-1569. Synonym: RNA polymerase ii subunit 1, RNA polymerase ii subunit b1, DNA-directed RNA polymerase iii largest subunit, RNA polymerase ii

Source:

Saccharomyces cerevisiae s288c. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: nrd1, ynl251c, n0868. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 559292

NMR struc:

20 models

Authors:

K.Kubicek,H.Cerna,J.Pasulka,P.Holub,D.Hrossova,F.Loehr,C.Hofr, S.Vanacova,R.Stefl

Key ref:

K.Kubicek et al. (2012). Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1. Genes Dev, 26, 1891-1896. PubMed id: 22892239

Date:

17-Jan-12 Release date: 26-Dec-12

Protein chain

P53617  (NRD1_YEAST) -  Protein NRD1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 575 a.a.

Struc: 154 a.a.*

Protein chain

P04050  (RPB1_YEAST) -  DNA-directed RNA polymerase II subunit RPB1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1733 a.a.

Struc: 14 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chain B: E.C.2.7.7.6 - DNA-directed Rna polymerase.
• Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

Genes Dev 26:1891-1896 (2012)

PubMed id: 22892239

Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1.

K.Kubicek, H.Cerna, P.Holub, J.Pasulka, D.Hrossova, F.Loehr, C.Hofr, S.Vanacova, R.Stefl.

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.