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| <StructureSection load='6s1l' size='340' side='right'caption='[[6s1l]], [[Resolution|resolution]] 1.94Å' scene=''> | | <StructureSection load='6s1l' size='340' side='right'caption='[[6s1l]], [[Resolution|resolution]] 1.94Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6s1l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S1L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6s1l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S1L FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mis16, hat2, SPCC1672.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</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]] 1.94Å</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=6s1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s1l OCA], [http://pdbe.org/6s1l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s1l RCSB], [http://www.ebi.ac.uk/pdbsum/6s1l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s1l 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=6s1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s1l OCA], [https://pdbe.org/6s1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s1l RCSB], [https://www.ebi.ac.uk/pdbsum/6s1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s1l ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/HAT2_SCHPO HAT2_SCHPO]] Regulatory subunit of the histone acetylase B (HAT-B) complex (By similarity). The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing (By similarity). Component of the CENP-A recruiting complex that ensures the integrity of mitotic spindles through maintenance of kinetochore factors mis6/CENP-I and cnp1/CENP-A (PubMed:15369671, PubMed:24774534, PubMed:24789708, PubMed:25375240). Maintains the deacetylated state of histones specifically in the central core of the centromeres (PubMed:15369671).[UniProtKB:P39984]<ref>PMID:15369671</ref> <ref>PMID:24774534</ref> <ref>PMID:24789708</ref> <ref>PMID:25375240</ref> | + | [https://www.uniprot.org/uniprot/HAT2_SCHPO HAT2_SCHPO] Regulatory subunit of the histone acetylase B (HAT-B) complex (By similarity). The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing (By similarity). Component of the CENP-A recruiting complex that ensures the integrity of mitotic spindles through maintenance of kinetochore factors mis6/CENP-I and cnp1/CENP-A (PubMed:15369671, PubMed:24774534, PubMed:24789708, PubMed:25375240). Maintains the deacetylated state of histones specifically in the central core of the centromeres (PubMed:15369671).[UniProtKB:P39984]<ref>PMID:15369671</ref> <ref>PMID:24774534</ref> <ref>PMID:24789708</ref> <ref>PMID:25375240</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 6s1l" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6s1l" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Cbs 356]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Korntner-Vetter, M]] | + | [[Category: Schizosaccharomyces pombe]] |
- | [[Category: Lefevre, S]] | + | [[Category: Korntner-Vetter M]] |
- | [[Category: Singleton, M R]]
| + | [[Category: Lefevre S]] |
- | [[Category: Cell cycle]] | + | [[Category: Singleton MR]] |
- | [[Category: Centromere mitosis wd40 histone chaperone]] | + | |
| Structural highlights
Function
HAT2_SCHPO Regulatory subunit of the histone acetylase B (HAT-B) complex (By similarity). The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing (By similarity). Component of the CENP-A recruiting complex that ensures the integrity of mitotic spindles through maintenance of kinetochore factors mis6/CENP-I and cnp1/CENP-A (PubMed:15369671, PubMed:24774534, PubMed:24789708, PubMed:25375240). Maintains the deacetylated state of histones specifically in the central core of the centromeres (PubMed:15369671).[UniProtKB:P39984][1] [2] [3] [4]
Publication Abstract from PubMed
Centromeric chromatin in fission yeast is distinguished by the presence of nucleosomes containing the histone H3 variant Cnp1(CENP-A) Cell cycle-specific deposition of Cnp1 requires the Mis16-Mis18-Mis19 complex, which is thought to direct recruitment of Scm3-chaperoned Cnp1/histone H4 dimers to DNA. Here, we present the structure of the essential Mis18 partner protein Mis19 and describe its interaction with Mis16, revealing a bipartite-binding site. We provide data on the stoichiometry and overall architecture of the complex and provide detailed insights into the Mis18-Mis19 interface.
Subunit interactions and arrangements in the fission yeast Mis16-Mis18-Mis19 complex.,Korntner-Vetter M, Lefevre S, Hu XW, George R, Singleton MR Life Sci Alliance. 2019 Aug 1;2(4). pii: 2/4/e201900408. doi:, 10.26508/lsa.201900408. Print 2019 Aug. PMID:31371524[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hayashi T, Fujita Y, Iwasaki O, Adachi Y, Takahashi K, Yanagida M. Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres. Cell. 2004 Sep 17;118(6):715-29. PMID:15369671 doi:http://dx.doi.org/10.1016/j.cell.2004.09.002
- ↑ Hayashi T, Ebe M, Nagao K, Kokubu A, Sajiki K, Yanagida M. Schizosaccharomyces pombe centromere protein Mis19 links Mis16 and Mis18 to recruit CENP-A through interacting with NMD factors and the SWI/SNF complex. Genes Cells. 2014 Jul;19(7):541-54. doi: 10.1111/gtc.12152. Epub 2014 Apr 29. PMID:24774534 doi:http://dx.doi.org/10.1111/gtc.12152
- ↑ Subramanian L, Toda NR, Rappsilber J, Allshire RC. Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly. Open Biol. 2014 Apr 30;4:140043. doi: 10.1098/rsob.140043. PMID:24789708 doi:http://dx.doi.org/10.1098/rsob.140043
- ↑ Hirai H, Arai K, Kariyazono R, Yamamoto M, Sato M. The kinetochore protein Kis1/Eic1/Mis19 ensures the integrity of mitotic spindles through maintenance of kinetochore factors Mis6/CENP-I and CENP-A. PLoS One. 2014 Nov 6;9(11):e111905. doi: 10.1371/journal.pone.0111905., eCollection 2014. PMID:25375240 doi:http://dx.doi.org/10.1371/journal.pone.0111905
- ↑ Korntner-Vetter M, Lefevre S, Hu XW, George R, Singleton MR. Subunit interactions and arrangements in the fission yeast Mis16-Mis18-Mis19 complex. Life Sci Alliance. 2019 Aug 1;2(4). pii: 2/4/e201900408. doi:, 10.26508/lsa.201900408. Print 2019 Aug. PMID:31371524 doi:http://dx.doi.org/10.26508/lsa.201900408
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