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6xwt

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Revision as of 07:29, 8 April 2020

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

Structural highlights

6xwt is a 6 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	cid, CENP-A, CG13329 (DROME), His4r, BcDNA:RH52884, Dmel\CG3379, FBtr0082962, H4r, His4-88CD, His4R, CG3379, Dmel_CG3379 (DROME), cal1, CAL1, Cal1, CLD2, Dmel\CG5148, CG5148, Dmel_CG5148 (DROME)
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] [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]

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.

References

↑ 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
↑ 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
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6xwt"

@@ Line 3: / Line 3: @@
 <StructureSection load='6xwt' size='340' side='right'caption='[[6xwt]], [[Resolution|resolution]] 3.47&Aring;' 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>
+<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>
-</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>
+</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>
+<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>
 </table>
 == Function ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Drome]]
 [[Category: Large Structures]]
 [[Category: Abad, M A]]

6xwt

From Proteopedia

Revision as of 07:29, 8 April 2020

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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