4X2H

Sac3N peptide bound to Mex67:Mtr2

4X2H の概要

• エントリーDOI: 10.2210/pdb4x2h/pdb
• 分子名称: Putative mRNA export protein, Putative uncharacterized protein, SER-SER-VAL-PHE-GLY-ALA-PRO-ALA, ... (4 entities in total)
• 機能のキーワード: mrna nuclear export, trex-2, transcription
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44612.26

構造登録者

Aibara, S.,Valkov, E.,Stewart, M. (登録日: 2014-11-26, 公開日: 2015-06-17, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)