View source for 6xws


==Crystal Structure of Drosophila CAL1 1-160 bound to CENP-A/H4==
<StructureSection load='6xws' size='340' side='right'caption='[[6xws]], [[Resolution|resolution]] 4.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xws]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XWS 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]] 4.36&#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=6xws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xws OCA], [https://pdbe.org/6xws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xws RCSB], [https://www.ebi.ac.uk/pdbsum/6xws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xws ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CID_DROME CID_DROME] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore (PubMed:11483958, PubMed:16839185). Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation (PubMed:24703848, PubMed:11483958, PubMed:16839185). May serve as an epigenetic mark that propagates centromere identity through replication and cell division (PubMed:11483958, PubMed:16839185).<ref>PMID:11483958</ref> <ref>PMID:16839185</ref> <ref>PMID:24703848</ref> 
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== Publication Abstract from PubMed ==
Centromeres are microtubule attachment sites on chromosomes defined by the enrichment of histone variant CENP-A-containing nucleosomes. To preserve centromere identity, CENP-A must be escorted to centromeres by a CENP-A-specific chaperone for deposition. Despite this essential requirement, many eukaryotes differ in the composition of players involved in centromere maintenance, highlighting the plasticity of this process. In humans, CENP-A recognition and centromere targeting are achieved by HJURP and the Mis18 complex, respectively. Using X-ray crystallography, we here show how Drosophila CAL1, an evolutionarily distinct CENP-A histone chaperone, binds both CENP-A and the centromere receptor CENP-C without the requirement for the Mis18 complex. While an N-terminal CAL1 fragment wraps around CENP-A/H4 through multiple physical contacts, a C-terminal CAL1 fragment directly binds a CENP-C cupin domain dimer. Although divergent at the primary structure level, CAL1 thus binds CENP-A/H4 using evolutionarily conserved and adaptive structural principles. The CAL1 binding site on CENP-C is strategically positioned near the cupin dimerisation interface, restricting binding to just one CAL1 molecule per CENP-C dimer. Overall, by demonstrating how CAL1 binds CENP-A/H4 and CENP-C, we provide key insights into the minimalistic principles underlying centromere maintenance.

Structural basis for centromere maintenance by Drosophila CENP-A chaperone CAL1.,Medina-Pritchard B, Lazou V, Zou J, Byron O, Abad MA, Rappsilber J, Heun P, Jeyaprakash AA EMBO J. 2020 Mar 5:e103234. doi: 10.15252/embj.2019103234. PMID:32134144<ref>PMID:32134144</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6xws" style="background-color:#fffaf0;"></div>

==See Also==
*[[Histone 3D structures|Histone 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Abad MA]]
[[Category: Byron O]]
[[Category: Heun P]]
[[Category: Jeyaprakash AA]]
[[Category: Lazou V]]
[[Category: Medina-Pritchard B]]
[[Category: Rappsilber J]]
[[Category: Zou J]]