3oak: Difference between revisions
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[[ | ==Crystal structure of a Spn1 (Iws1)-Spt6 complex== | ||
<StructureSection load='3oak' size='340' side='right' caption='[[3oak]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== 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> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o8z|3o8z]]</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'>[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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Elongation factor|Elongation factor]] | *[[Elongation factor|Elongation factor]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Close, D | [[Category: Close, D]] | ||
[[Category: Hill, C P | [[Category: Hill, C P]] | ||
[[Category: McDonald, S M | [[Category: McDonald, S M]] | ||
[[Category: Nucleus]] | [[Category: Nucleus]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
[[Category: Transcription factor complex]] | [[Category: Transcription factor complex]] | ||
Revision as of 15:10, 9 December 2014
Crystal structure of a Spn1 (Iws1)-Spt6 complexCrystal structure of a Spn1 (Iws1)-Spt6 complex
Structural highlights
Publication Abstract from PubMedEukaryotic 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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