5l3t
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5l3t is ON HOLD Authors: Stewart, M., Aibara, S. Description: Structure of the Saccharomyces cerevisiae TREX-2 complex [[Category: Unreleased Struc...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Saccharomyces cerevisiae TREX-2 complex== | |
| + | <StructureSection load='5l3t' size='340' side='right'caption='[[5l3t]], [[Resolution|resolution]] 4.93Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5l3t]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L3T FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.927Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5l3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l3t OCA], [https://pdbe.org/5l3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l3t RCSB], [https://www.ebi.ac.uk/pdbsum/5l3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l3t ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SAC3_YEAST SAC3_YEAST] Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket.<ref>PMID:12411502</ref> <ref>PMID:12702719</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 Sac3M region (residues approximately 100-551), and the other in which Cdc31 and two Sus1 chains bind to the Sac3CID region (residues approximately 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 Sac3M region extend considerably further towards the N-terminus than previously thought, and also indicate that this region and Sac3CID:Sus1:Cdc31 region of the S. cerevisiae complex are structurally independent. Although the density visible accounted for only approximately 100kDa, a 5.3A resolution cryo-EM reconstruction was obtained of the M-region of TREX-2 that showed an additional three putative alpha-helices extending towards the Sac3 N-terminus and these helices were also seen in a 4.9A resolution structure obtained by X-ray crystallography. SUMMARY STATEMENT: We describe the expression, purification and structural characterization of the S. cerevisiae TREX-2 complex and demonstrate that the Sac3 TPR-like repeats are more extensive than previously thought and that the M- and CID-regions do not appear to have a defined spatial orientation. | ||
| - | + | The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region.,Aibara S, Bai XC, Stewart M J Struct Biol. 2016 Jul 12. pii: S1047-8477(16)30148-4. doi:, 10.1016/j.jsb.2016.07.007. PMID:27422657<ref>PMID:27422657</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Aibara | + | <div class="pdbe-citations 5l3t" style="background-color:#fffaf0;"></div> |
| - | [[Category: Stewart | + | |
| + | ==See Also== | ||
| + | *[[Proteasome 3D structures|Proteasome 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Aibara S]] | ||
| + | [[Category: Stewart M]] | ||
Current revision
Structure of the Saccharomyces cerevisiae TREX-2 complex
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