2yfw: Difference between revisions
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== | ==Heterotetramer structure of Kluyveromyces lactis Cse4,H4== | ||
<StructureSection load='2yfw' size='340' side='right' caption='[[2yfw]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2yfw' size='340' side='right'caption='[[2yfw]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yfw]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2yfw]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YFW FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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=2yfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yfw OCA], [https://pdbe.org/2yfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yfw RCSB], [https://www.ebi.ac.uk/pdbsum/2yfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yfw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CENPA_KLULA CENPA_KLULA] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Histone|Histone]] | *[[Histone 3D structures|Histone 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Kluyveromyces lactis NRRL Y-1140]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Cho US]] | ||
[[Category: | [[Category: Harrison SC]] | ||
Latest revision as of 13:51, 20 December 2023
Heterotetramer structure of Kluyveromyces lactis Cse4,H4Heterotetramer structure of Kluyveromyces lactis Cse4,H4
Structural highlights
FunctionCENPA_KLULA Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). Publication Abstract from PubMedA specialized nucleosome is a component of all eukaryotic kinetochores. The core of this nucleosome contains a centromere-specific histone, CENP-A (the Cse4 gene product in budding yeast), instead of the usual H3. Assembly of a centromeric nucleosome depends on a specific chaperone, called Scm3 in yeast and HJURP in higher eukaryotes. We describe here the structure of a complex formed by an N-terminal fragment of Scm3 with the histone-fold domains of Cse4, and H4, all prepared as recombinant proteins derived from the budding yeast Kluyveromyces lactis. The contacts of Scm3 with Cse4 explain its selectivity for the centromere-specific histone; key residues at the interface are conserved in HJURP, indicating a common mechanism for centromeric-histone deposition. We also report the structure of a (Cse4 : H4)(2) heterotetramer; comparison with the structure of the Scm3:Cse4:H4 complex shows that tetramer formation and DNA-binding require displacement of Scm3 from the nucleosome core. The two structures together suggest that specific contacts between the chaperone and Cse4, rather than an altered overall structure of the nucleosome core, determine the selective presence of Cse4 at centromeres. Recognition of the centromere-specific histone Cse4 by the chaperone Scm3.,Cho US, Harrison SC Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9367-71. Epub 2011 May 23. PMID:21606327[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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