7l7q
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Ctf3c with Ulp2-KIM== |
| - | <StructureSection load='7l7q' size='340' side='right'caption='[[7l7q]]' scene=''> | + | <StructureSection load='7l7q' size='340' side='right'caption='[[7l7q]], [[Resolution|resolution]] 3.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7l7q]] is a 3 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=7L7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L7Q FirstGlance]. <br> |
| - | </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=7l7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l7q OCA], [https://pdbe.org/7l7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l7q RCSB], [https://www.ebi.ac.uk/pdbsum/7l7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l7q ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</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=7l7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l7q OCA], [https://pdbe.org/7l7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l7q RCSB], [https://www.ebi.ac.uk/pdbsum/7l7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l7q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CENPH_YEAST CENPH_YEAST] Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.<ref>PMID:9862478</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The step-by-step process of chromosome segregation defines the stages of the cell cycle. In eukaryotes, signals controlling these steps converge upon the kinetochore, a multiprotein assembly that connects spindle microtubules to chromosomal centromeres. Kinetochores control and adapt to major chromosomal transactions, including replication of centromeric DNA, biorientation of sister centromeres on the metaphase spindle, and transit of sister chromatids into daughter cells during anaphase. Although the mechanisms that ensure tight microtubule coupling at anaphase are at least partly understood, kinetochore adaptations that support other cell cycle transitions are not. We report here a mechanism that enables regulated control of kinetochore sumoylation. A conserved surface of the Ctf3/CENP-I kinetochore protein provides a binding site for Ulp2, the nuclear enzyme that removes SUMO chains from modified substrates. Ctf3 mutations that disable Ulp2 recruitment cause elevated inner kinetochore sumoylation and defective chromosome segregation. The location of the site within the assembled kinetochore suggests coordination between sumoylation and other cell cycle-regulated processes. | ||
| + | |||
| + | Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore.,Quan Y, Hinshaw SM, Wang PC, Harrison SC, Zhou H J Cell Biol. 2021 Aug 2;220(8):e202012149. doi: 10.1083/jcb.202012149. Epub 2021 , Jun 3. PMID:34081091<ref>PMID:34081091</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7l7q" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
| + | [[Category: Harrison SC]] | ||
| + | [[Category: Hinshaw SM]] | ||
Current revision
Ctf3c with Ulp2-KIM
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