6s1l
From Proteopedia
(Difference between revisions)
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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. 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 [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> |
| - | </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> | + | </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> |
| + | <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> | ||
</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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:31371524</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6s1l" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Cbs 356]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Korntner-Vetter, M]] | [[Category: Korntner-Vetter, M]] | ||
Revision as of 17:34, 14 August 2019
Structure of fission yeast Mis16
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