5G5P

Structure of the Saccharomyces cerevisiae TREX-2 complex

5G5P の概要

• エントリーDOI: 10.2210/pdb5g5p/pdb
• EMDBエントリー: 3440
• 分子名称: NUCLEAR MRNA EXPORT PROTEIN SAC3, NUCLEAR MRNA EXPORT PROTEIN THP1, 26S PROTEASOME COMPLEX SUBUNIT SEM1, ... (4 entities in total)
• 機能のキーワード: transport protein, mrna, mrna export
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 361926.64

構造登録者

Aibara, S.,Bai, X.C.,Stewart, M. (登録日: 2016-05-26, 公開日: 2016-11-23, 最終更新日: 2024-05-08)

主引用文献

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-, 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

実験手法

ELECTRON MICROSCOPY (5.3 Å)