6h8q: Difference between revisions

New page: '''Unreleased structure''' The entry 6h8q is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 6h8q is ON HOLD
==Structural basis for Scc3-dependent cohesin recruitment to chromatin==
<StructureSection load='6h8q' size='340' side='right' caption='[[6h8q]], [[Resolution|resolution]] 3.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6h8q]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H8Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H8Q FirstGlance]. <br>
</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=6h8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h8q OCA], [http://pdbe.org/6h8q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h8q RCSB], [http://www.ebi.ac.uk/pdbsum/6h8q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h8q ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SCC3_YEAST SCC3_YEAST]] Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the MCD1/SCC1 subunit of the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. [[http://www.uniprot.org/uniprot/SCC1_YEAST SCC1_YEAST]] Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by ESP1 and dissociates from chromatin, allowing sister chromatids to segregate.<ref>PMID:9335333</ref> <ref>PMID:9335334</ref> <ref>PMID:9491073</ref> <ref>PMID:10403247</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cohesin ring complex is required for numerous chromosomal transactions, including sister chromatid cohesion, DNA damage repair and transcriptional regulation. How cohesin engages its chromatin substrate has remained an unresolved question. We show here, by determining a crystal structure of the budding yeast cohesin HEAT-repeat subunit Scc3 bound to a fragment of the Scc1 kleisin subunit and DNA, that Scc3 and Scc1 together form a composite DNA interaction module. The Scc3-Scc1 subcomplex engages double-strand DNA through a conserved, positively charged surface. We demonstrate that this conserved domain is required for DNA binding by Scc3-Scc1 in vitro, as well as for the enrichment of cohesin on chromosomes and for cell viability. These findings suggest that the Scc3-Scc1 DNA-binding interface plays a central role in the recruitment of cohesin complexes to chromosomes and therefore for cohesin to faithfully execute its functions during cell division.


Authors:  
Structural basis for Scc3-dependent cohesin recruitment to chromatin.,Li Y, Muir K, Bowler MW, Metz J, Haering CH, Panne D Elife. 2018 Aug 15;7. pii: 38356. doi: 10.7554/eLife.38356. PMID:30109982<ref>PMID:30109982</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6h8q" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Li, Y]]
[[Category: Muir, K]]
[[Category: Panne, D]]
[[Category: Cell cycle]]
[[Category: Cohesin cell proliferation scc3 dna binding]]

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