This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


6s29

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='6s29' size='340' side='right'caption='[[6s29]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='6s29' size='340' side='right'caption='[[6s29]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6s29]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S29 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6s29]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356] and [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S29 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></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]), mis19, eic1, kis1, SPBC27B12.02, SPBC30B4.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=6s29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s29 OCA], [http://pdbe.org/6s29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s29 RCSB], [http://www.ebi.ac.uk/pdbsum/6s29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s29 ProSAT]</span></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=6s29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s29 OCA], [http://pdbe.org/6s29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s29 RCSB], [http://www.ebi.ac.uk/pdbsum/6s29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s29 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/MIS19_SCHPO MIS19_SCHPO]] 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:24774534, PubMed:24789708, PubMed:25375240). Links mis16 and mis18 to recruit CENP-A through interacting with non-sense-mediated mRNA decay (NMD) factors and the SWI/SNF complex (PubMed:24774534). Links also mis18 with the CCAN/mis6/ctf19 complex to promote CENP-A assembly (PubMed:24789708).<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> [[http://www.uniprot.org/uniprot/MIS19_SCHPO MIS19_SCHPO]] 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:24774534, PubMed:24789708, PubMed:25375240). Links mis16 and mis18 to recruit CENP-A through interacting with non-sense-mediated mRNA decay (NMD) factors and the SWI/SNF complex (PubMed:24774534). Links also mis18 with the CCAN/mis6/ctf19 complex to promote CENP-A assembly (PubMed:24789708).<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.
 +
 +
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>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6s29" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Cbs 356]]
 +
[[Category: Fission yeast]]
[[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-Mis19 complex

PDB ID 6s29

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6s29"
Personal tools