2xpl

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<StructureSection load='2xpl' size='340' side='right'caption='[[2xpl]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='2xpl' size='340' side='right'caption='[[2xpl]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xpl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enccn Enccn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XPL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xpl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Encephalitozoon_cuniculi Encephalitozoon cuniculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XPL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xpn|2xpn]], [[2xpp|2xpp]], [[2xpo|2xpo]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=2xpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xpl OCA], [https://pdbe.org/2xpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xpl RCSB], [https://www.ebi.ac.uk/pdbsum/2xpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xpl ProSAT]</span></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=2xpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xpl OCA], [https://pdbe.org/2xpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xpl RCSB], [https://www.ebi.ac.uk/pdbsum/2xpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xpl ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8SUS7_ENCCU Q8SUS7_ENCCU]
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Binding of elongation factor Spt6 to Iws1 provides an effective means for coupling eukaryotic mRNA synthesis, chromatin remodelling and mRNA export. We show that an N-terminal region of Spt6 (Spt6N) is responsible for interaction with Iws1. The crystallographic structures of Encephalitozoon cuniculi Iws1 and the Iws1/Spt6N complex reveal two conserved binding subdomains in Iws1. The first subdomain (one HEAT repeat; HEAT subdomain) is a putative phosphoprotein-binding site most likely involved in an Spt6-independent function of Iws1. The second subdomain (two ARM repeats; ARM subdomain) specifically recognizes a bipartite N-terminal region of Spt6. Mutations that alter this region of Spt6 cause severe phenotypes in vivo. Importantly, the ARM subdomain of Iws1 is conserved in several transcription factors, including TFIIS, Elongin A and Med26. We show that the homologous region in yeast TFIIS enables this factor to interact with SAGA and the Mediator subunits Spt8 and Med13, suggesting the molecular basis for TFIIS recruitment at promoters. Taken together, our results provide new structural information about the Iws1/Spt6 complex and reveal a novel interaction domain used for the formation of transcription networks.
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The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26.,Diebold ML, Koch M, Loeliger E, Cura V, Winston F, Cavarelli J, Romier C EMBO J. 2010 Dec 1;29(23):3979-91. Epub 2010 Nov 5. PMID:21057455<ref>PMID:21057455</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2xpl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enccn]]
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[[Category: Encephalitozoon cuniculi]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cavarelli, J]]
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[[Category: Cavarelli J]]
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[[Category: Cura, V]]
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[[Category: Cura V]]
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[[Category: Diebold, M L]]
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[[Category: Diebold M-L]]
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[[Category: Koch, M]]
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[[Category: Koch M]]
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[[Category: Romier, C]]
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[[Category: Romier C]]
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[[Category: Elongation]]
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[[Category: Mrna export]]
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[[Category: Rna polymerase ii]]
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[[Category: Transcription]]
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Current revision

Crystal structure of Iws1(Spn1) conserved domain from Encephalitozoon cuniculi

PDB ID 2xpl

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