View source for 4uzw


==High-resolution NMR structures of the domains of Saccharomyces cerevisiae Tho1==
<StructureSection load='4uzw' size='340' side='right'caption='[[4uzw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4uzw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UZW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=4uzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uzw OCA], [https://pdbe.org/4uzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uzw RCSB], [https://www.ebi.ac.uk/pdbsum/4uzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uzw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THO1_YEAST THO1_YEAST] Unknown; suppressor of the transcriptional defect of HPR1 by overexpression.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
THO is a multi-protein complex involved in the formation of messenger ribonuclear particles (mRNPs) by coupling transcription with mRNA processing and export. THO is thought to be formed from five subunits, Tho2p, Hpr1p, Tex1p, Mft1p and Thp2p, and recent work has determined a low-resolution structure of the complex [Poulsen et al. (2014), PLoS One, 9, e103470]. A number of additional proteins are thought to be involved in the formation of mRNP in yeast, including Tho1, which has been shown to bind RNA in vitro and is recruited to actively transcribed chromatin in vivo in a THO-complex and RNA-dependent manner. Tho1 is known to contain a SAP domain at the N-terminus, but the ability to suppress the expression defects of the hpr1Delta mutant of THO was shown to reside in the RNA-binding C-terminal region. In this study, high-resolution structures of both the N-terminal DNA-binding SAP domain and C-terminal RNA-binding domain have been determined.

High-resolution NMR structures of the domains of Saccharomyces cerevisiae Tho1.,Jacobsen JO, Allen MD, Freund SM, Bycroft M Acta Crystallogr F Struct Biol Commun. 2016 Jun 1;72(Pt 6):500-6. doi:, 10.1107/S2053230X16007597. Epub 2016 May 23. PMID:27303905<ref>PMID:27303905</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4uzw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Allen MD]]
[[Category: Bycroft M]]
[[Category: Freund SMV]]
[[Category: Jacobsen JOB]]