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'''Unreleased structure'''


The entry 6ypc is ON HOLD  until Paper Publication
==Crystal structure of the kinetochore subunits H/I/K/T/W penta-complex from S. cerevisiae at 2.9 angstroms==
<StructureSection load='6ypc' size='340' side='right'caption='[[6ypc]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ypc]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YPC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#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=6ypc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ypc OCA], [https://pdbe.org/6ypc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ypc RCSB], [https://www.ebi.ac.uk/pdbsum/6ypc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ypc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CENPK_YEAST CENPK_YEAST] Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.<ref>PMID:9987135</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Kinetochores are large multi-subunit complexes that attach centromeric chromatin to microtubules of the mitotic spindle, enabling sister chromatid segregation in mitosis. The inner kinetochore constitutive centromere associated network (CCAN) complex assembles onto the centromere-specific Cenp-A nucleosome (Cenp-ANuc), thereby coupling the centromere to the microtubule-binding outer kinetochore. CCAN is a conserved 14-16 subunit complex composed of discrete modules. Here, we determined the crystal structure of the Saccharomyces cerevisiae Cenp-HIKHead-TW sub-module, revealing how Cenp-HIK and Cenp-TW interact at the conserved Cenp-HIKHead-Cenp-TW interface. A major interface is formed by the C-terminal anti-parallel alpha-helices of the histone fold extension (HFE) of the Cenp-T histone fold domain (HFD) combining with alpha-helix H3 of Cenp-K to create a compact three alpha-helical bundle. We fitted the Cenp-HIKHead-TW sub-module to the previously determined cryo-EM map of the S. cerevisiae CCAN-Cenp-ANuc complex. This showed that the HEAT repeat domain of Cenp-IHead and C-terminal HFD of Cenp-T of the Cenp-HIKHead-TW sub-module interact with the nucleosome DNA gyre at a site close to the Cenp-ANuc dyad axis. Our structure provides a framework for understanding how Cenp-T links centromeric Cenp-ANuc to the outer kinetochore through its HFD and N-terminal Ndc80-binding motif, respectively.


Authors: Bellini, D., Zhang, Z., Barford, D.
Crystal structure of the Cenp-HIKHead-TW sub-module of the inner kinetochore CCAN complex.,Zhang Z, Bellini D, Barford D Nucleic Acids Res. 2020 Nov 4;48(19):11172-11184. doi: 10.1093/nar/gkaa772. PMID:32976599<ref>PMID:32976599</ref>


Description: Crystal structure of the kinetochore subunits H/I/K/T/W penta-complex from S. cerevisiae at 2.9 angstroms
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Zhang, Z]]
<div class="pdbe-citations 6ypc" style="background-color:#fffaf0;"></div>
[[Category: Barford, D]]
== References ==
[[Category: Bellini, D]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Barford D]]
[[Category: Bellini D]]
[[Category: Zhang Z]]

Latest revision as of 16:32, 24 January 2024

Crystal structure of the kinetochore subunits H/I/K/T/W penta-complex from S. cerevisiae at 2.9 angstromsCrystal structure of the kinetochore subunits H/I/K/T/W penta-complex from S. cerevisiae at 2.9 angstroms

Structural highlights

6ypc is a 5 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CENPK_YEAST Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.[1]

Publication Abstract from PubMed

Kinetochores are large multi-subunit complexes that attach centromeric chromatin to microtubules of the mitotic spindle, enabling sister chromatid segregation in mitosis. The inner kinetochore constitutive centromere associated network (CCAN) complex assembles onto the centromere-specific Cenp-A nucleosome (Cenp-ANuc), thereby coupling the centromere to the microtubule-binding outer kinetochore. CCAN is a conserved 14-16 subunit complex composed of discrete modules. Here, we determined the crystal structure of the Saccharomyces cerevisiae Cenp-HIKHead-TW sub-module, revealing how Cenp-HIK and Cenp-TW interact at the conserved Cenp-HIKHead-Cenp-TW interface. A major interface is formed by the C-terminal anti-parallel alpha-helices of the histone fold extension (HFE) of the Cenp-T histone fold domain (HFD) combining with alpha-helix H3 of Cenp-K to create a compact three alpha-helical bundle. We fitted the Cenp-HIKHead-TW sub-module to the previously determined cryo-EM map of the S. cerevisiae CCAN-Cenp-ANuc complex. This showed that the HEAT repeat domain of Cenp-IHead and C-terminal HFD of Cenp-T of the Cenp-HIKHead-TW sub-module interact with the nucleosome DNA gyre at a site close to the Cenp-ANuc dyad axis. Our structure provides a framework for understanding how Cenp-T links centromeric Cenp-ANuc to the outer kinetochore through its HFD and N-terminal Ndc80-binding motif, respectively.

Crystal structure of the Cenp-HIKHead-TW sub-module of the inner kinetochore CCAN complex.,Zhang Z, Bellini D, Barford D Nucleic Acids Res. 2020 Nov 4;48(19):11172-11184. doi: 10.1093/nar/gkaa772. PMID:32976599[2]

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

References

  1. ↑ Poddar A, Roy N, Sinha P. MCM21 and MCM22, two novel genes of the yeast Saccharomyces cerevisiae are required for chromosome transmission. Mol Microbiol. 1999 Jan;31(1):349-60. PMID:9987135
  2. ↑ Zhang Z, Bellini D, Barford D. Crystal structure of the Cenp-HIKHead-TW sub-module of the inner kinetochore CCAN complex. Nucleic Acids Res. 2020 Nov 4;48(19):11172-11184. PMID:32976599 doi:10.1093/nar/gkaa772

6ypc, resolution 2.90Å

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