8u8d

Cryo-EM structure of the TREX-2 complex in complex with the N-terminal motif of Sub2

spinqualitylabelsall models 8u8d, resolution 3.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8u8d is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.04Å Ligands: PBF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed mRNAs are packaged with proteins into messenger ribonucleoprotein complexes (mRNPs) in the nucleus. mRNP assembly and export are of fundamental importance for all eukaryotic gene expression. Before export to the cytoplasm, mRNPs undergo dynamic remodeling governed by the DEAD-box helicase DDX39B (yeast Sub2). DDX39B/Sub2 primarily functions in the nucleus and leaves the mRNP prior to export through the nuclear pore complex; however, the underlying mechanisms remain elusive. Here, we identify the conserved TREX-2 complex as the long-sought factor that facilitates DDX39B/Sub2 to complete the mRNP remodeling cycle. Our crystallographic and cryoelectron microscopy (cryo-EM) analyses demonstrate that TREX-2 modulates the activities of DDX39B/Sub2 through multiple interactions. Critically, a conserved "trigger loop" from TREX-2 splits the two RecA domains of DDX39B/Sub2 and promotes the removal of DDX39B/Sub2 from mRNP. Our findings suggest that TREX-2 coordinates with DDX39B/Sub2 and the human export receptor NXF1-NXT1 (yeast Mex67-Mtr2) to complete the final steps of nuclear mRNP assembly. Structures and mRNP remodeling mechanism of the TREX-2 complex.,Xie Y, Clarke BP, Xie D, Mei M, Bhat P, Hill PS, Angelos AE, Cagatay T, Haider M, Collier SE, Chambers MG, Aksenova V, Dasso M, Fontoura BMA, Ren Y Structure. 2025 Jan 17:S0969-2126(24)00581-1. doi: 10.1016/j.str.2024.12.019. PMID:39862860 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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