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==Crystal structure of a Spn1 (Iws1)-Spt6 complex==
==Crystal structure of a Spn1 (Iws1)-Spt6 complex==
<StructureSection load='3oak' size='340' side='right' caption='[[3oak]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3oak' size='340' side='right'caption='[[3oak]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3oak]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OAK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OAK FirstGlance]. <br>
<table><tr><td colspan='2'>[[3oak]] is a 4 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=3OAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OAK FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o8z|3o8z]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IWS1, SPN1, YPR133C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), SPT6, CRE2, SSN20, YGR116W, G6169 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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=3oak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oak OCA], [https://pdbe.org/3oak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oak RCSB], [https://www.ebi.ac.uk/pdbsum/3oak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oak ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oak OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oak RCSB], [http://www.ebi.ac.uk/pdbsum/3oak PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/IWS1_YEAST IWS1_YEAST] Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post-recruitment and recruitment steps of transcription.<ref>PMID:12524336</ref> <ref>PMID:12556496</ref>  
Eukaryotic transcription and mRNA processing depend upon the coordinated interactions of many proteins, including Spn1 and Spt6, which are conserved across eukaryotes, are essential for viability, and associate with each other in some of their biologically important contexts. Here we report crystal structures of the Spn1 core alone and in complex with the binding determinant of Spt6. Mutating interface residues greatly diminishes binding in vitro and causes strong phenotypes in vivo, including a defect in maintaining repressive chromatin. Overexpression of Spn1 partially suppresses the defects caused by an spt6 mutation affecting the Spn1 interface, indicating that the Spn1-Spt6 interaction is important for managing chromatin. Spt6 binds nucleosomes directly in vitro, and this interaction is blocked by Spn1, providing further mechanistic insight into the function of the interaction. These data thereby reveal the structural and biochemical bases of molecular interactions that function in the maintenance of chromatin structure.
 
Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding.,McDonald SM, Close D, Xin H, Formosa T, Hill CP Mol Cell. 2010 Dec 10;40(5):725-35. Epub 2010 Nov 25. PMID:21094070<ref>PMID:21094070</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Elongation factor|Elongation factor]]
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Close, D]]
[[Category: Close D]]
[[Category: Hill, C P]]
[[Category: Hill CP]]
[[Category: McDonald, S M]]
[[Category: McDonald SM]]
[[Category: Nucleus]]
[[Category: Transcription]]
[[Category: Transcription factor complex]]

Latest revision as of 13:04, 14 February 2024

Crystal structure of a Spn1 (Iws1)-Spt6 complexCrystal structure of a Spn1 (Iws1)-Spt6 complex

Structural highlights

3oak is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IWS1_YEAST Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post-recruitment and recruitment steps of transcription.[1] [2]

See Also

References

  1. ↑ Fischbeck JA, Kraemer SM, Stargell LA. SPN1, a conserved gene identified by suppression of a postrecruitment-defective yeast TATA-binding protein mutant. Genetics. 2002 Dec;162(4):1605-16. PMID:12524336
  2. ↑ Lindstrom DL, Squazzo SL, Muster N, Burckin TA, Wachter KC, Emigh CA, McCleery JA, Yates JR 3rd, Hartzog GA. Dual roles for Spt5 in pre-mRNA processing and transcription elongation revealed by identification of Spt5-associated proteins. Mol Cell Biol. 2003 Feb;23(4):1368-78. PMID:12556496

3oak, resolution 2.15Å

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