6YPC
Crystal structure of the kinetochore subunits H/I/K/T/W penta-complex from S. cerevisiae at 2.9 angstroms
Summary for 6YPC
| Entry DOI | 10.2210/pdb6ypc/pdb |
| Descriptor | Inner kinetochore subunit MCM22, Inner kinetochore subunit MCM16, Inner kinetochore subunit CNN1, ... (6 entities in total) |
| Functional Keywords | kinetochore, cenp complex, centromeres, chromosome segregation, cell cycle |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) More |
| Total number of polymer chains | 5 |
| Total formula weight | 99169.21 |
| Authors | Bellini, D.,Zhang, Z.,Barford, D. (deposition date: 2020-04-15, release date: 2020-09-16, Last modification date: 2024-01-24) |
| Primary citation | Zhang, Z.,Bellini, D.,Barford, D. Crystal structure of the Cenp-HIKHead-TW sub-module of the inner kinetochore CCAN complex. Nucleic Acids Res., 48:11172-11184, 2020 Cited by PubMed Abstract: 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 α-helices of the histone fold extension (HFE) of the Cenp-T histone fold domain (HFD) combining with α-helix H3 of Cenp-K to create a compact three α-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. PubMed: 32976599DOI: 10.1093/nar/gkaa772 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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