6xws
From Proteopedia
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==Crystal Structure of Drosophila CAL1 1-160 bound to CENP-A/H4== | ==Crystal Structure of Drosophila CAL1 1-160 bound to CENP-A/H4== | ||
| - | <StructureSection load='6xws' size='340' side='right'caption='[[6xws]]' scene=''> | + | <StructureSection load='6xws' size='340' side='right'caption='[[6xws]], [[Resolution|resolution]] 4.36Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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 [ | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.36Å</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> | </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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6xws" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Histone 3D structures|Histone 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Abad MA]] | [[Category: Abad MA]] | ||
Current revision
Crystal Structure of Drosophila CAL1 1-160 bound to CENP-A/H4
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