5L3T

Structure of the Saccharomyces cerevisiae TREX-2 complex

Summary for 5L3T

• Entry DOI: 10.2210/pdb5l3t/pdb
• Descriptor: Nuclear mRNA export protein SAC3, Nuclear mRNA export protein THP1, 26S proteasome complex subunit SEM1, ... (5 entities in total)
• Functional Keywords: nuclear export, trex-2 complex, sac3, thp1, transport protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 6
• Total formula weight: 218068.55

Authors

Stewart, M.,Aibara, S. (deposition date: 2016-05-24, release date: 2016-07-27, Last modification date: 2024-01-10)

Primary citation

Aibara, S.,Bai, X.C.,Stewart, M.
The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region.
J. Struct. Biol., 195:316-324, 2016

PubMed Abstract: Transcription-export complex 2 (TREX-2 complex) facilitates the localization of actively transcribing genes to the nuclear periphery and also functions to contribute to the generation of export-competent mRNPs through interactions with the general mRNA nuclear export factor Mex67:Mtr2. The TREX-2 complex is based on a Sac3 scaffold to which Thp1, Sem1, Cdc31, and Sus1 bind. TREX-2 can be subdivided into two modules: one, in which Thp1 and Sem1 bind to the Sac3(M) region (residues ∼100-551), and the other in which Cdc31 and two Sus1 chains bind to the Sac3(CID) region (residues ∼710-805). Complementary structural analyses using X-ray crystallography, electron microscopy, and small-angle X-ray scattering of the Saccharomyces cerevisiae TREX-2 complex, expressed using Baculovirus-infected Sf9 cells, have indicated that the TPR-like repeats of the Sac3(M) region extend considerably further towards the N-terminus than previously thought, and also indicate that this region and Sac3(CID):Sus1:Cdc31 region of the S. cerevisiae complex are structurally independent. Although the density visible accounted for only ∼100kDa, a 5.3Å resolution cryo-EM reconstruction was obtained of the M-region of TREX-2 that showed an additional three putative α-helices extending towards the Sac3 N-terminus and these helices were also seen in a 4.9Å resolution structure obtained by X-ray crystallography.

PubMed: 27422657
DOI: 10.1016/j.jsb.2016.07.007

Experimental method

X-RAY DIFFRACTION (4.927 Å)