4uvj: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<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=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4uvj]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4uvj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4UVJ FirstGlance]. <br> | ||
</td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uvj OCA], [https://pdbe.org/4uvj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uvj RCSB], [https://www.ebi.ac.uk/pdbsum/4uvj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uvj ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 21: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: | [[Category: Lowe J]] | ||
[[Category: | [[Category: Nasmyth K]] | ||
[[Category: | [[Category: Roig MB]] | ||
Revision as of 10:42, 29 March 2023
Cohesin subunit Scc3 from yeast, 674-1072Cohesin subunit Scc3 from yeast, 674-1072
Structural highlights
FunctionSCC3_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
|
| ||||||||||||||