6xwt: Difference between revisions

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<StructureSection load='6xwt' size='340' side='right'caption='[[6xwt]], [[Resolution|resolution]] 3.47&Aring;' scene=''>
<StructureSection load='6xwt' size='340' side='right'caption='[[6xwt]], [[Resolution|resolution]] 3.47&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6xwt]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. 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://proteopedia.org/fgij/fg.htm?mol=6XWT FirstGlance]. <br>
<table><tr><td colspan='2'>[[6xwt]] is a 6 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=6XWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XWT FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cid, CENP-A, CG13329 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), His4r, BcDNA:RH52884, Dmel\CG3379, FBtr0082962, H4r, His4-88CD, His4R, CG3379, Dmel_CG3379 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), cal1, CAL1, Cal1, CLD2, Dmel\CG5148, CG5148, Dmel_CG5148 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.47&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6xwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwt OCA], [https://pdbe.org/6xwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xwt RCSB], [https://www.ebi.ac.uk/pdbsum/6xwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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]
[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6xwt" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6xwt" style="background-color:#fffaf0;"></div>
==See Also==
*[[Histone 3D structures|Histone 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drome]]
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Abad, M A]]
[[Category: Abad MA]]
[[Category: Byron, O]]
[[Category: Byron O]]
[[Category: Heun, P]]
[[Category: Heun P]]
[[Category: Jeyaprakash, A A]]
[[Category: Jeyaprakash AA]]
[[Category: Lazou, V]]
[[Category: Lazou V]]
[[Category: Medina-Pritchard, B]]
[[Category: Medina-Pritchard B]]
[[Category: Rappsilber, J]]
[[Category: Rappsilber J]]
[[Category: Zou, J]]
[[Category: Zou J]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Centromere]]
[[Category: Kinetochore]]

Latest revision as of 16:14, 24 January 2024

drosophila melanogaster CENP-A/H4 bound to N-terminal CAL1 fragmentdrosophila melanogaster CENP-A/H4 bound to N-terminal CAL1 fragment

Structural highlights

6xwt is a 6 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.47Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3]

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[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Blower MD, Karpen GH. The role of Drosophila CID in kinetochore formation, cell-cycle progression and heterochromatin interactions. Nat Cell Biol. 2001 Aug;3(8):730-9. doi: 10.1038/35087045. PMID:11483958 doi:http://dx.doi.org/10.1038/35087045
  2. Blower MD, Daigle T, Kaufman T, Karpen GH. Drosophila CENP-A mutations cause a BubR1-dependent early mitotic delay without normal localization of kinetochore components. PLoS Genet. 2006 Jul;2(7):e110. Epub 2006 Jun 5. PMID:16839185 doi:http://dx.doi.org/05-PLGE-RA-0358R2
  3. Mathew V, Pauleau AL, Steffen N, Bergner A, Becker PB, Erhardt S. The histone-fold protein CHRAC14 influences chromatin composition in response to DNA damage. Cell Rep. 2014 Apr 24;7(2):321-330. doi: 10.1016/j.celrep.2014.03.008. Epub 2014 , Apr 3. PMID:24703848 doi:http://dx.doi.org/10.1016/j.celrep.2014.03.008
  4. Medina-Pritchard B, Lazou V, Zou J, Byron O, Abad MA, Rappsilber J, Heun P, Jeyaprakash AA. Structural basis for centromere maintenance by Drosophila CENP-A chaperone CAL1. EMBO J. 2020 Mar 5:e103234. doi: 10.15252/embj.2019103234. PMID:32134144 doi:http://dx.doi.org/10.15252/embj.2019103234

6xwt, resolution 3.47Å

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