PDBsum entry 4x2o

Transport protein

PDB id: 4x2o

Contents

Protein chains

179 a.a.

175 a.a.

Ligands

SER-SER-VAL-PHE-GLY-ALA-PRO-ALA

Waters ×275

PDB id:

4x2o

Name:

Transport protein

Title:

Sac3n peptide bound to mex67:mtr2

Structure:

Putative mRNA export protein. Chain: a. Fragment: unp residues 365-564. Engineered: yes. Putative uncharacterized protein. Chain: b. Fragment: unp residues 12-187. Engineered: yes. Putative sac3 family protein.

Source:

Chaetomium thermophilum. Organism_taxid: 759272. Strain: dsm 1495 / cbs 144.50 / imi 039719. Gene: ctht_0059630. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ctht_0065500. Gene: ctht_0066750. Expression_system_taxid: 562

Resolution:

1.85Å R-factor: 0.164 R-free: 0.201

Authors:

S.Aibara,E.Valkov,M.Stewart

Key ref:

L.Dimitrova et al. (2015). Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2. Structure, 23, 1246-1257. PubMed id: 26051714 DOI: 10.1016/j.str.2015.05.002

Date:

26-Nov-14 Release date: 17-Jun-15

Protein chain

G0SET4  (G0SET4_CHATD) -  Putative mRNA export protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 657 a.a.

Struc: 179 a.a.*

Protein chain

G0SG92  (G0SG92_CHATD) -  NTF2 domain-containing protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 187 a.a.

Struc: 175 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

DOI no: 10.1016/j.str.2015.05.002

Structure 23:1246-1257 (2015)

PubMed id: 26051714

Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2.

L.Dimitrova, E.Valkov, S.Aibara, D.Flemming, S.H.McLaughlin, E.Hurt, M.Stewart.

ABSTRACT

The TREX-2 complex integrates mRNA nuclear export into the gene expression pathway and is based on a Sac3 scaffold to which Thp1, Sem1, Sus1, and Cdc31 bind. TREX-2 also binds the mRNA nuclear export factor, Mex67:Mtr2, through the Sac3 N-terminal region (Sac3N). Here, we characterize Chaetomium thermophilum TREX-2, show that the in vitro reconstituted complex has an annular structure, and define the structural basis for interactions between Sac3, Sus1, Cdc31, and Mex67:Mtr2. Crystal structures show that the binding of C. thermophilum Sac3N to the Mex67 NTF2-like domain (Mex67(NTF2L)) is mediated primarily through phenylalanine residues present in a series of repeating sequence motifs that resemble those seen in many nucleoporins, and Mlp1 also binds Mex67:Mtr2 using a similar motif. Deletion of Sac3N generated growth and mRNA export defects in Saccharomyces cerevisiae, and we propose TREX-2 and Mlp1 function to facilitate export by concentrating mature messenger ribonucleoparticles at the nuclear pore entrance.