6OUA
Cryo-EM structure of the yeast Ctf3 complex
Summary for 6OUA
Entry DOI | 10.2210/pdb6oua/pdb |
Related | 6NUW |
EMDB information | 0523 20200 |
Descriptor | Inner kinetochore subunit CTF3, Inner kinetochore subunit MCM16, Inner kinetochore subunit MCM22 (3 entities in total) |
Functional Keywords | kinetochore, chromosome, cryo-em, cell cycle |
Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
Total number of polymer chains | 3 |
Total formula weight | 133931.05 |
Authors | Hinshaw, S.M.,Harrison, S.C. (deposition date: 2019-05-04, release date: 2019-05-15, Last modification date: 2025-06-04) |
Primary citation | Hinshaw, S.M.,Dates, A.N.,Harrison, S.C. The structure of the yeast Ctf3 complex. Elife, 8:-, 2019 Cited by PubMed Abstract: Kinetochores are the chromosomal attachment points for spindle microtubules. They are also signaling hubs that control major cell cycle transitions and coordinate chromosome folding. Most well-studied eukaryotes rely on a conserved set of factors, which are divided among two loosely-defined groups, for these functions. Outer kinetochore proteins contact microtubules or regulate this contact directly. Inner kinetochore proteins designate the kinetochore assembly site by recognizing a specialized nucleosome containing the H3 variant Cse4/CENP-A. We previously determined the structure, resolved by cryo-electron microscopy (cryo-EM), of the yeast Ctf19 complex (Ctf19c, homologous to the vertebrate CCAN), providing a high-resolution view of inner kinetochore architecture (Hinshaw and Harrison, 2019). We now extend these observations by reporting a near-atomic model of the Ctf3 complex, the outermost Ctf19c sub-assembly seen in our original cryo-EM density. The model is sufficiently well-determined by the new data to enable molecular interpretation of Ctf3 recruitment and function. PubMed: 31194673DOI: 10.7554/eLife.48215 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.18 Å) |
Structure validation
Download full validation report
