View source for 5suq


==Crystal structure of the THO-Sub2 complex==
<StructureSection load='5suq' size='340' side='right'caption='[[5suq]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5suq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SUQ 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]] 6&#8491;</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=5suq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5suq OCA], [https://pdbe.org/5suq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5suq RCSB], [https://www.ebi.ac.uk/pdbsum/5suq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5suq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUB2_YEAST SUB2_YEAST] ATP-binding RNA helicase component of the TREX complex involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 plays also a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity.<ref>PMID:10077188</ref> <ref>PMID:11156602</ref> <ref>PMID:11156603</ref> <ref>PMID:11156604</ref> <ref>PMID:11463828</ref> <ref>PMID:11675790</ref> <ref>PMID:11696331</ref> <ref>PMID:11979277</ref> <ref>PMID:12034490</ref> <ref>PMID:12093753</ref> <ref>PMID:12417727</ref> <ref>PMID:12871933</ref> <ref>PMID:15942929</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
mRNA is cotranscrptionally processed and packaged into messenger ribonucleoprotein particles (mRNPs) in the nucleus. Prior to export through the nuclear pore, mRNPs undergo several obligatory remodeling reactions. In yeast, one of these reactions involves loading of the mRNA-binding protein Yra1 by the DEAD-box ATPase Sub2 as assisted by the hetero-pentameric THO complex. To obtain molecular insights into reaction mechanisms, we determined crystal structures of two relevant complexes: a THO hetero-pentamer bound to Sub2 at 6.0 A resolution; and Sub2 associated with an ATP analogue, RNA, and a C-terminal fragment of Yra1 (Yra1-C) at 2.6 A resolution. We found that the 25 nm long THO clamps Sub2 in a half-open configuration; in contrast, when bound to the ATP analogue, RNA and Yra1-C, Sub2 assumes a closed conformation. Both THO and Yra1-C stimulated Sub2's intrinsic ATPase activity. We propose that THO surveys common landmarks in each nuclear mRNP to localize Sub2 for targeted loading of Yra1.

Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1.,Ren Y, Schmiege P, Blobel G Elife. 2017 Jan 6;6. pii: e20070. doi: 10.7554/eLife.20070. PMID:28059701<ref>PMID:28059701</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5suq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Blobel G]]
[[Category: Ren Y]]