PDBsum entry 5o1x

Transcription

PDB id: 5o1x

Contents

Protein chain

162 a.a.

Ligands

EDO ×7

SCN ×8

Waters ×138

PDB id:

5o1x

Name:

Transcription

Title:

Structure of nrd1 RNA binding domain

Structure:

Protein nrd1. Chain: a. Fragment: unp residues 290-468. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: nrd1, ynl251c, n0868. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.60Å R-factor: 0.179 R-free: 0.208

Authors:

E.Franco-Echevarria,J.M.Perez-Canadillas,B.Gonzalez

Key ref:

E.Franco-Echevarría et al. (2017). The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition. Nucleic Acids Res, 45, 10293-10305. PubMed id: 28973465

Date:

19-May-17 Release date: 02-Aug-17

Protein chain

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

Seq: 575 a.a.

Struc: 162 a.a.

Nucleic Acids Res 45:10293-10305 (2017)

PubMed id: 28973465

The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition.

E.Franco-Echevarría, N.González-Polo, S.Zorrilla, S.Martínez-Lumbreras, C.M.Santiveri, R.Campos-Olivas, M.Sánchez, O.Calvo, B.González, J.M.Pérez-Cañadillas.

ABSTRACT

Transcription termination of non-coding RNAs is regulated in yeast by a complex of three RNA binding proteins: Nrd1, Nab3 and Sen1. Nrd1 is central in this process by interacting with Rbp1 of RNA polymerase II, Trf4 of TRAMP and GUAA/G terminator sequences. We lack structural data for the last of these binding events. We determined the structures of Nrd1 RNA binding domain and its complexes with three GUAA-containing RNAs, characterized RNA binding energetics and tested rationally designed mutants in vivo. The Nrd1 structure shows an RRM domain fused with a second α/β domain that we name split domain (SD), because it is formed by two non-consecutive segments at each side of the RRM. The GUAA interacts with both domains and with a pocket of water molecules, trapped between the two stacking adenines and the SD. Comprehensive binding studies demonstrate for the first time that Nrd1 has a slight preference for GUAA over GUAG and genetic and functional studies suggest that Nrd1 RNA binding domain might play further roles in non-coding RNAs transcription termination.