4uvj: Difference between revisions
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==Cohesin subunit Scc3 from yeast, 674-1072== | ==Cohesin subunit Scc3 from yeast, 674-1072== | ||
<StructureSection load='4uvj' size='340' side='right' caption='[[4uvj]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4uvj' size='340' side='right' caption='[[4uvj]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<table><tr><td colspan='2'>[[4uvj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UVJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UVJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[4uvj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UVJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UVJ FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uvk|4uvk]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uvk|4uvk]]</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=4uvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uvj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uvj RCSB], [http://www.ebi.ac.uk/pdbsum/4uvj PDBsum]</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=4uvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uvj OCA], [http://pdbe.org/4uvj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uvj RCSB], [http://www.ebi.ac.uk/pdbsum/4uvj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uvj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4uvj" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 20:18, 5 August 2016
Cohesin subunit Scc3 from yeast, 674-1072Cohesin subunit Scc3 from yeast, 674-1072
Structural highlights
Function[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. Publication Abstract from PubMedSister chromatid cohesion involves entrapment of sister DNAs by a cohesin ring created through association of a kleisin subunit (Scc1) with ATPase heads of Smc1/Smc3 heterodimers. Cohesin's association with chromatin involves subunits recruited by Scc1: Wapl, Pds5, and Scc3/SA, in addition to Scc2/4 loading complex. Unlike Pds5, Wapl, and Scc2/4, Scc3s are encoded by all eukaryotic genomes. Here, a crystal structure of Scc3 reveals a hook-shaped protein composed of tandem alpha helices. Its N-terminal domain contains a conserved and essential surface (CES) present even in organisms lacking Pds5, Wapl, and Scc2/4, while its C-terminal domain binds a section of the kleisin Scc1. Scc3 turns over in G2/M while maintaining cohesin's association with chromosomes and it promotes de-acetylation of Smc3 upon Scc1 cleavage. Structure and function of cohesin's Scc3/SA regulatory subunit.,Roig MB, Lowe J, Chan KL, Beckouet F, Metson J, Nasmyth K FEBS Lett. 2014 Aug 27. pii: S0014-5793(14)00617-6. doi:, 10.1016/j.febslet.2014.08.015. PMID:25171859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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