View source for 5ktb


==Structure of a complex between S. cerevisiae Csm1 and Mam1==
<StructureSection load='5ktb' size='340' side='right'caption='[[5ktb]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ktb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4emc 4emc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KTB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.05&#8491;</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=5ktb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ktb OCA], [https://pdbe.org/5ktb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ktb RCSB], [https://www.ebi.ac.uk/pdbsum/5ktb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ktb ProSAT]</span></td></tr>
</table>
== Function ==
[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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Saccharomyces cerevisiae monopolin complex directs proper chromosome segregation in meiosis I by mediating co-orientation of sister kinetochores on the meiosis I spindle. The monopolin subunits Csm1 and Lrs4 form a V-shaped complex that may directly crosslink sister kinetochores. We report here biochemical characterization of the monopolin complex subunits Mam1 and Hrr25 and of the complete four-protein monopolin complex. By purifying monopolin subcomplexes with different subunit combinations, we have determined the stoichiometry and overall architecture of the full monopolin complex. We have determined the crystal structure of Csm1 bound to a Mam1 fragment, showing how Mam1 wraps around the Csm1 dimer and alters the stoichiometry of kinetochore-protein binding by Csm1. We further show that the kinase activity of Hrr25 is altered by Mam1 binding, and we identify Hrr25 phosphorylation sites on Mam1 that may affect monopolin complex stability and/or kinetochore binding in meiosis.

Molecular architecture of the yeast monopolin complex.,Corbett KD, Harrison SC Cell Rep. 2012 Jun 28;1(6):583-9. Epub 2012 Jun 21. PMID:22813733<ref>PMID:22813733</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ktb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Corbett KD]]
[[Category: Harrison SC]]