6seg: Difference between revisions

Latest revision as of 13:14, 22 May 2024

Class1: CENP-A nucleosome in complex with CENP-C central regionClass1: CENP-A nucleosome in complex with CENP-C central region

6seg, resolution 3.10Å

Structural highlights

6seg is a 10 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.1Å
Experimental data:	Check
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CENPA_HUMAN Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro).^[1] ^[2]

Publication Abstract from PubMed

Centromeres are defined epigenetically by nucleosomes containing the histone H3 variant CENP-A, upon which the constitutive centromere-associated network of proteins (CCAN) is built. CENP-C is considered to be a central organizer of the CCAN. We provide new molecular insights into the structure of human CENP-A nucleosomes, in isolation and in complex with the CENP-C central region (CENP-C(CR) ), the main CENP-A binding module of human CENP-C. We establish that the short alphaN helix of CENP-A promotes DNA flexibility at the nucleosome ends, independently of the sequence it wraps. Furthermore, we show that, in vitro, two regions of human CENP-C (CENP-C(CR) and CENP-C(motif) ) both bind exclusively to the CENP-A nucleosome. We find CENP-C(CR) to bind with high affinity due to an extended hydrophobic area made up of CENP-A(V) (532) and CENP-A(V) (533) . Importantly, we identify two key conformational changes within the CENP-A nucleosome upon CENP-C binding. First, the loose DNA wrapping of CENP-A nucleosomes is further exacerbated, through destabilization of the H2A C-terminal tail. Second, CENP-C(CR) rigidifies the N-terminal tail of H4 in the conformation favoring H4(K20) monomethylation, essential for a functional centromere.

CENP-C unwraps the human CENP-A nucleosome through the H2A C-terminal tail.,Ali-Ahmad A, Bilokapic S, Schafer IB, Halic M, Sekulic N EMBO Rep. 2019 Oct 4;20(10):e48913. doi: 10.15252/embr.201948913. Epub 2019 Sep, 2. PMID:31475439^[3]

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

References

↑ Sekulic N, Bassett EA, Rogers DJ, Black BE. The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres. Nature. 2010 Aug 25. PMID:20739937 doi:10.1038/nature09323
↑ Hu H, Liu Y, Wang M, Fang J, Huang H, Yang N, Li Y, Wang J, Yao X, Shi Y, Li G, Xu RM. Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. Genes Dev. 2011 May 1;25(9):901-6. Epub 2011 Apr 8. PMID:21478274 doi:10.1101/gad.2045111
↑ Ali-Ahmad A, Bilokapic S, Schafer IB, Halic M, Sekulic N. CENP-C unwraps the human CENP-A nucleosome through the H2A C-terminal tail. EMBO Rep. 2019 Oct 4;20(10):e48913. doi: 10.15252/embr.201948913. Epub 2019 Sep, 2. PMID:31475439 doi:http://dx.doi.org/10.15252/embr.201948913

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OCA

[1] Sekulic N, Bassett EA, Rogers DJ, Black BE. The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres. Nature. 2010 Aug 25. PMID:20739937 doi:10.1038/nature09323

[2] Hu H, Liu Y, Wang M, Fang J, Huang H, Yang N, Li Y, Wang J, Yao X, Shi Y, Li G, Xu RM. Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. Genes Dev. 2011 May 1;25(9):901-6. Epub 2011 Apr 8. PMID:21478274 doi:10.1101/gad.2045111

[3] Ali-Ahmad A, Bilokapic S, Schafer IB, Halic M, Sekulic N. CENP-C unwraps the human CENP-A nucleosome through the H2A C-terminal tail. EMBO Rep. 2019 Oct 4;20(10):e48913. doi: 10.15252/embr.201948913. Epub 2019 Sep, 2. PMID:31475439 doi:http://dx.doi.org/10.15252/embr.201948913

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <SX load='6seg' size='340' side='right' viewer='molstar' caption='[[6seg]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6seg]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SEG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SEG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6seg]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SEG FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CENPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST2H2AA3, H2AFO, HIST2H2AA, HIST2H2AA4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H2BC, H2BFL, HIST1H2BE, H2BFH, HIST1H2BF, H2BFG, HIST1H2BG, H2BFA, HIST1H2BI, H2BFK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#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=6seg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6seg OCA], [http://pdbe.org/6seg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6seg RCSB], [http://www.ebi.ac.uk/pdbsum/6seg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6seg 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=6seg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6seg OCA], [https://pdbe.org/6seg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6seg RCSB], [https://www.ebi.ac.uk/pdbsum/6seg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6seg ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CENPA_HUMAN CENPA_HUMAN]] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro).<ref>PMID:20739937</ref> <ref>PMID:21478274</ref>
+[https://www.uniprot.org/uniprot/CENPA_HUMAN CENPA_HUMAN] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro).<ref>PMID:20739937</ref> <ref>PMID:21478274</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 </div>
 <div class="pdbe-citations 6seg" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Centromere protein 3D structure|Centromere protein 3D structure]]
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ali-Ahmad, A]]
+[[Category: Synthetic construct]]
-[[Category: Bilokapic, S]]
+[[Category: Ali-Ahmad A]]
-[[Category: Halic, M]]
+[[Category: Bilokapic S]]
-[[Category: Schafer, I B]]
+[[Category: Halic M]]
-[[Category: Sekulic, N]]
+[[Category: Schafer IB]]
-[[Category: Cenp-a]]
+[[Category: Sekulic N]]
-[[Category: Centromere]]
-[[Category: Centromeric chromatin]]
-[[Category: Nuclear protein]]
-[[Category: Nucleosome]]

6seg: Difference between revisions

Latest revision as of 13:14, 22 May 2024

Class1: CENP-A nucleosome in complex with CENP-C central regionClass1: CENP-A nucleosome in complex with CENP-C central region

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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6seg: Difference between revisions

Latest revision as of 13:14, 22 May 2024

Class1: CENP-A nucleosome in complex with CENP-C central regionClass1: CENP-A nucleosome in complex with CENP-C central region

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Search