6tly: Difference between revisions
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<StructureSection load='6tly' size='340' side='right'caption='[[6tly]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6tly' size='340' side='right'caption='[[6tly]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6tly]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TLY OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6tly]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bodsa Bodsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TLY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSAL_50690 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=75058 BODSA])</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=6tly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tly OCA], [https://pdbe.org/6tly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tly RCSB], [https://www.ebi.ac.uk/pdbsum/6tly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tly ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The kinetochore is the macromolecular protein complex that assembles onto centromeric DNA and binds spindle microtubules. Evolutionarily divergent kinetoplastids have an unconventional set of kinetochore proteins. It remains unknown how kinetochores assemble at centromeres in these organisms. Here, we characterize KKT2 and KKT3 in the kinetoplastid parasite Trypanosoma brucei. In addition to the N-terminal kinase domain and C-terminal divergent polo boxes, these proteins have a central domain of unknown function. We show that KKT2 and KKT3 are important for the localization of several kinetochore proteins and that their central domains are sufficient for centromere localization. Crystal structures of the KKT2 central domain from two divergent kinetoplastids reveal a unique zinc-binding domain (termed the CL domain for centromere localization), which promotes its kinetochore localization in T. brucei. Mutations in the equivalent domain in KKT3 abolish its kinetochore localization and function. Our work shows that the unique central domains play a critical role in mediating the centromere localization of KKT2 and KKT3. | |||
Kinetoplastid kinetochore proteins KKT2 and KKT3 have unique centromere localization domains.,Marciano G, Ishii M, Nerusheva OO, Akiyoshi B J Cell Biol. 2021 Aug 2;220(8). pii: 212224. doi: 10.1083/jcb.202101022. Epub, 2021 Jun 3. PMID:34081090<ref>PMID:34081090</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6tly" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bodsa]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Akiyoshi, B]] | [[Category: Akiyoshi, B]] | ||
Latest revision as of 17:51, 17 June 2021
Crystal structure of the unconventional kinetochore protein Bodo saltans KKT2 central domainCrystal structure of the unconventional kinetochore protein Bodo saltans KKT2 central domain
Structural highlights
Publication Abstract from PubMedThe kinetochore is the macromolecular protein complex that assembles onto centromeric DNA and binds spindle microtubules. Evolutionarily divergent kinetoplastids have an unconventional set of kinetochore proteins. It remains unknown how kinetochores assemble at centromeres in these organisms. Here, we characterize KKT2 and KKT3 in the kinetoplastid parasite Trypanosoma brucei. In addition to the N-terminal kinase domain and C-terminal divergent polo boxes, these proteins have a central domain of unknown function. We show that KKT2 and KKT3 are important for the localization of several kinetochore proteins and that their central domains are sufficient for centromere localization. Crystal structures of the KKT2 central domain from two divergent kinetoplastids reveal a unique zinc-binding domain (termed the CL domain for centromere localization), which promotes its kinetochore localization in T. brucei. Mutations in the equivalent domain in KKT3 abolish its kinetochore localization and function. Our work shows that the unique central domains play a critical role in mediating the centromere localization of KKT2 and KKT3. Kinetoplastid kinetochore proteins KKT2 and KKT3 have unique centromere localization domains.,Marciano G, Ishii M, Nerusheva OO, Akiyoshi B J Cell Biol. 2021 Aug 2;220(8). pii: 212224. doi: 10.1083/jcb.202101022. Epub, 2021 Jun 3. PMID:34081090[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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