3b0b: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of the chicken CENP-S/CENP-X complex== | ==Crystal structure of the chicken CENP-S/CENP-X complex== | ||
<StructureSection load='3b0b' size='340' side='right' caption='[[3b0b]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='3b0b' size='340' side='right'caption='[[3b0b]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3b0b]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3b0b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B0B FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b0c|3b0c]], [[3b0d|3b0d]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3b0c|3b0c]], [[3b0d|3b0d]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CENP-S ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CENP-S ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK]), CENP-X ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=3b0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b0b OCA], [https://pdbe.org/3b0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b0b RCSB], [https://www.ebi.ac.uk/pdbsum/3b0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b0b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 20: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Centromere protein|Centromere protein]] | *[[Centromere protein 3D structure|Centromere protein 3D structure]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 26: | Line 26: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Chick]] | [[Category: Chick]] | ||
[[Category: Large Structures]] | |||
[[Category: Cheeseman, I M]] | [[Category: Cheeseman, I M]] | ||
[[Category: Fukagawa, T]] | [[Category: Fukagawa, T]] | ||
Revision as of 14:19, 5 January 2022
Crystal structure of the chicken CENP-S/CENP-X complexCrystal structure of the chicken CENP-S/CENP-X complex
Structural highlights
Publication Abstract from PubMedThe multiprotein kinetochore complex must assemble at a specific site on each chromosome to achieve accurate chromosome segregation. Defining the nature of the DNA-protein interactions that specify the position of the kinetochore and provide a scaffold for kinetochore formation remain key goals. Here, we demonstrate that the centromeric histone-fold-containing CENP-T-W and CENP-S-X complexes coassemble to form a stable CENP-T-W-S-X heterotetramer. High-resolution structural analysis of the individual complexes and the heterotetramer reveals similarity to other histone fold-containing complexes including canonical histones within a nucleosome. The CENP-T-W-S-X heterotetramer binds to and supercoils DNA. Mutants designed to compromise heterotetramerization or the DNA-protein contacts around the heterotetramer strongly reduce the DNA binding and supercoiling activities in vitro and compromise kinetochore assembly in vivo. These data suggest that the CENP-T-W-S-X complex forms a unique nucleosome-like structure to generate contacts with DNA, extending the "histone code" beyond canonical nucleosome proteins. CENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Fold.,Nishino T, Takeuchi K, Gascoigne KE, Suzuki A, Hori T, Oyama T, Morikawa K, Cheeseman IM, Fukagawa T Cell. 2012 Feb 3;148(3):487-501. PMID:22304917[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||