4uvj: Difference between revisions
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<tr><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><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> | ||
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== Publication Abstract from PubMed == | |||
Sister 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<ref>PMID:25171859</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 10:21, 10 September 2014
Cohesin subunit Scc3 from yeast, 674-1072Cohesin subunit Scc3 from yeast, 674-1072
Structural highlights
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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