6s1l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:33, 24 January 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='6s1l' size='340' side='right'caption='[[6s1l]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
<StructureSection load='6s1l' size='340' side='right'caption='[[6s1l]], [[Resolution|resolution]] 1.94&Aring;' 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 [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='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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</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;">
 +
== 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 6s1l" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 13: Line 26:
</StructureSection>
</StructureSection>
[[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]]
+

Current revision

Structure of fission yeast Mis16

PDB ID 6s1l

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/6s1l"
Personal tools