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6OUA

Cryo-EM structure of the yeast Ctf3 complex

Summary for 6OUA
Entry DOI10.2210/pdb6oua/pdb
Related6NUW
EMDB information0523 20200
DescriptorInner kinetochore subunit CTF3, Inner kinetochore subunit MCM16, Inner kinetochore subunit MCM22 (3 entities in total)
Functional Keywordskinetochore, chromosome, cryo-em, cell cycle
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Total number of polymer chains3
Total formula weight133931.05
Authors
Hinshaw, S.M.,Harrison, S.C. (deposition date: 2019-05-04, release date: 2019-05-15, Last modification date: 2025-06-04)
Primary citationHinshaw, 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: 31194673
DOI: 10.7554/eLife.48215
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.18 Å)
Structure validation

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건을2025-08-27부터공개중

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