2veq: Difference between revisions
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<StructureSection load='2veq' size='340' side='right'caption='[[2veq]], [[Resolution|resolution]] 2.49Å' scene=''> | <StructureSection load='2veq' size='340' side='right'caption='[[2veq]], [[Resolution|resolution]] 2.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2veq]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2veq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VEQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2veq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2veq OCA], [https://pdbe.org/2veq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2veq RCSB], [https://www.ebi.ac.uk/pdbsum/2veq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2veq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2veq" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2veq" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Centromere protein 3D structure|Centromere protein 3D structure]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:35, 30 March 2022
Insights into kinetochore-DNA interactions from the structure of Cep3pInsights into kinetochore-DNA interactions from the structure of Cep3p
Structural highlights
Publication Abstract from PubMedThe CBF3 complex is an essential core component of the budding yeast kinetochore and is required for the centromeric localization of all other kinetochore proteins. We determined the crystal structure of a large section of the protein Cep3 from CBF3, which is the only component with obvious DNA-binding motifs. The protein adopts a roughly bilobal shape, with an extended dimerization interface. The dimer has a large central channel that is sufficient to accommodate duplex B-form DNA. The zinc-finger domains emerge at the edges of the channel, and could bind to the DNA in a pseudo-symmetrical manner at degenerate half-sites in the centromeric sequence. We propose a mechanism for the modulation of DNA affinity by an acidic activator domain, which could be applicable to a wider family of transcription factors. Insights into kinetochore-DNA interactions from the structure of Cep3Delta.,Purvis A, Singleton MR EMBO Rep. 2008 Jan;9(1):56-62. Epub 2007 Dec 7. PMID:18064045[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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