6dei

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==Structure of Dse3-Csm1 complex==
==Structure of Dse3-Csm1 complex==
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<StructureSection load='6dei' size='340' side='right' caption='[[6dei]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='6dei' size='340' side='right'caption='[[6dei]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6dei]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DEI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6dei]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DEI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.699&#8491;</td></tr>
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<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=6dei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dei OCA], [http://pdbe.org/6dei PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dei RCSB], [http://www.ebi.ac.uk/pdbsum/6dei PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dei ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6dei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dei OCA], [https://pdbe.org/6dei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dei RCSB], [https://www.ebi.ac.uk/pdbsum/6dei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dei ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CSM1_YEAST CSM1_YEAST]] Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Plays also a mitotic role in DNA replication.<ref>PMID:11470404</ref> <ref>PMID:12689592</ref> <ref>PMID:15023545</ref> <ref>PMID:16487579</ref> <ref>PMID:18997772</ref> [[http://www.uniprot.org/uniprot/DSE3_YEAST DSE3_YEAST]] May be involved in the establishment of the daughter fate.
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[https://www.uniprot.org/uniprot/CSM1_YEAST CSM1_YEAST] Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Plays also a mitotic role in DNA replication.<ref>PMID:11470404</ref> <ref>PMID:12689592</ref> <ref>PMID:15023545</ref> <ref>PMID:16487579</ref> <ref>PMID:18997772</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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RWD domains mediate protein-protein interactions in a variety of pathways in eukaryotes. In budding yeast, the RWD domain protein Csm1 is particularly versatile, assembling key complexes in the nucleolus and at meiotic kinetochores through multiple protein interaction surfaces. Here, we reveal a third functional context for Csm1 by identifying a new Csm1-interacting protein, Dse3. We show that Dse3 interacts with Csm1 in a structurally equivalent manner to its known binding partners Mam1 and Ulp2, despite these three proteins' lack of overall sequence homology. We theorize that the unique "clamp" structure of Csm1 and the loose sequence requirements for Csm1 binding have led to its incorporation into at least three different structural/signaling pathways in budding yeast. This article is protected by copyright. All rights reserved.
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The budding-yeast RWD protein Csm1 scaffolds diverse protein complexes through a conserved structural mechanism.,Singh N, Corbett KD Protein Sci. 2018 Sep 25. doi: 10.1002/pro.3515. PMID:30252178<ref>PMID:30252178</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6dei" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Corbett, K D]]
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[[Category: Large Structures]]
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[[Category: Singh, N]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Daughter cell-specific protein]]
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[[Category: Corbett KD]]
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[[Category: Monopolin]]
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[[Category: Singh N]]
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[[Category: Protein binding-cell cycle complex]]
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Current revision

Structure of Dse3-Csm1 complex

PDB ID 6dei

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