5f0n: Difference between revisions
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The | ==Cohesin subunit Pds5== | ||
<StructureSection load='5f0n' size='340' side='right' caption='[[5f0n]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5f0n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F0N FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=5f0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f0n OCA], [http://pdbe.org/5f0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f0n RCSB], [http://www.ebi.ac.uk/pdbsum/5f0n PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sister chromatid cohesion is mediated by cohesin, whose Smc1, Smc3, and kleisin (Scc1) subunits form a ring structure that entraps sister DNAs. The ring is opened either by separase, which cleaves Scc1 during anaphase, or by a releasing activity involving Wapl, Scc3, and Pds5, which bind to Scc1 and open its interface with Smc3. We present crystal structures of Pds5 from the yeast L. thermotolerans in the presence and absence of the conserved Scc1 region that interacts with Pds5. Scc1 binds along the spine of the Pds5 HEAT repeat fold and is wedged between the spine and C-terminal hook of Pds5. We have isolated mutants that confirm the observed binding mode of Scc1 and verified their effect on cohesin by immunoprecipitation and calibrated ChIP-seq. The Pds5 structure also reveals architectural similarities to Scc3, the other large HEAT repeat protein of cohesin and, most likely, Scc2. | |||
Crystal Structure of the Cohesin Gatekeeper Pds5 and in Complex with Kleisin Scc1.,Lee BG, Roig MB, Jansma M, Petela N, Metson J, Nasmyth K, Lowe J Cell Rep. 2016 Mar 8;14(9):2108-15. doi: 10.1016/j.celrep.2016.02.020. Epub 2016 , Feb 25. PMID:26923598<ref>PMID:26923598</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5f0n" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Jansma, M]] | [[Category: Jansma, M]] | ||
[[Category: Lee, B | [[Category: Lee, B G]] | ||
[[Category: Lowe, J]] | [[Category: Lowe, J]] | ||
[[Category: Nasmyth, K]] | [[Category: Nasmyth, K]] | ||
[[Category: Cell cycle]] | |||
[[Category: Heat repeat cohesin subunit]] | |||
Revision as of 21:44, 12 May 2016
Cohesin subunit Pds5Cohesin subunit Pds5
Structural highlights
Publication Abstract from PubMedSister chromatid cohesion is mediated by cohesin, whose Smc1, Smc3, and kleisin (Scc1) subunits form a ring structure that entraps sister DNAs. The ring is opened either by separase, which cleaves Scc1 during anaphase, or by a releasing activity involving Wapl, Scc3, and Pds5, which bind to Scc1 and open its interface with Smc3. We present crystal structures of Pds5 from the yeast L. thermotolerans in the presence and absence of the conserved Scc1 region that interacts with Pds5. Scc1 binds along the spine of the Pds5 HEAT repeat fold and is wedged between the spine and C-terminal hook of Pds5. We have isolated mutants that confirm the observed binding mode of Scc1 and verified their effect on cohesin by immunoprecipitation and calibrated ChIP-seq. The Pds5 structure also reveals architectural similarities to Scc3, the other large HEAT repeat protein of cohesin and, most likely, Scc2. Crystal Structure of the Cohesin Gatekeeper Pds5 and in Complex with Kleisin Scc1.,Lee BG, Roig MB, Jansma M, Petela N, Metson J, Nasmyth K, Lowe J Cell Rep. 2016 Mar 8;14(9):2108-15. doi: 10.1016/j.celrep.2016.02.020. Epub 2016 , Feb 25. PMID:26923598[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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