4X2H

Sac3N peptide bound to Mex67:Mtr2

Summary for 4X2H

• Entry DOI: 10.2210/pdb4x2h/pdb
• Descriptor: Putative mRNA export protein, Putative uncharacterized protein, SER-SER-VAL-PHE-GLY-ALA-PRO-ALA, ... (4 entities in total)
• Functional Keywords: mrna nuclear export, trex-2, transcription
• Biological source: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); More
• Total number of polymer chains: 3
• Total formula weight: 44612.26

Authors

Aibara, S.,Valkov, E.,Stewart, M. (deposition date: 2014-11-26, release date: 2015-06-17, Last modification date: 2024-05-08)

Primary citation

Dimitrova, L.,Valkov, E.,Aibara, S.,Flemming, D.,McLaughlin, S.H.,Hurt, E.,Stewart, M.
Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2.
Structure, 23:1246-1257, 2015

PubMed 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.

PubMed: 26051714
DOI: 10.1016/j.str.2015.05.002

Experimental method

X-RAY DIFFRACTION (1.8 Å)