6xwt
From Proteopedia
(Difference between revisions)
m (Protected "6xwt" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==drosophila melanogaster CENP-A/H4 bound to N-terminal CAL1 fragment== | |
| + | <StructureSection load='6xwt' size='340' side='right'caption='[[6xwt]], [[Resolution|resolution]] 3.47Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6xwt]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6XWT FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6xwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwt OCA], [http://pdbe.org/6xwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xwt RCSB], [http://www.ebi.ac.uk/pdbsum/6xwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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> [[http://www.uniprot.org/uniprot/A0A0B4KFZ9_DROME A0A0B4KFZ9_DROME]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.[RuleBase:RU000528][SAAS:SAAS00581158] | ||
| + | <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 6xwt" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Abad, M A]] | ||
[[Category: Byron, O]] | [[Category: Byron, O]] | ||
| - | [[Category: Jeyaprakash, A.A]] | ||
[[Category: Heun, P]] | [[Category: Heun, P]] | ||
| + | [[Category: Jeyaprakash, A A]] | ||
[[Category: Lazou, V]] | [[Category: Lazou, V]] | ||
| - | [[Category: | + | [[Category: Medina-Pritchard, B]] |
| + | [[Category: Rappsilber, J]] | ||
| + | [[Category: Zou, J]] | ||
| + | [[Category: Cell cycle]] | ||
| + | [[Category: Cell division]] | ||
| + | [[Category: Centromere]] | ||
| + | [[Category: Kinetochore]] | ||
Revision as of 09:26, 1 April 2020
drosophila melanogaster CENP-A/H4 bound to N-terminal CAL1 fragment
| |||||||||||
