6FE8
Cryo-EM structure of the core Centromere Binding Factor 3 complex
Summary for 6FE8
| Entry DOI | 10.2210/pdb6fe8/pdb |
| Related | 6GSA |
| EMDB information | 0051 4241 |
| Descriptor | Centromere DNA-binding protein complex CBF3 subunit B, Suppressor of kinetochore protein 1, Centromere DNA-binding protein complex CBF3 subunit C (3 entities in total) |
| Functional Keywords | centromere, cdeiii-binding, lrr domain, dna binding protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 4 |
| Total formula weight | 220366.66 |
| Authors | Zhang, W.J.,Lukoynova, N.,Miah, S.,Vaughan, C.K. (deposition date: 2017-12-30, release date: 2018-08-01, Last modification date: 2019-12-11) |
| Primary citation | Zhang, W.,Lukoynova, N.,Miah, S.,Lucas, J.,Vaughan, C.K. Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10. Cell Rep, 24:744-754, 2018 Cited by PubMed Abstract: The centromere binding factor 3 (CBF3) complex binds the third centromere DNA element in organisms with point centromeres, such as S. cerevisiae. It is an essential complex for assembly of the kinetochore in these organisms, as it facilitates genetic centromere specification and allows association of all other kinetochore components. We determined high-resolution structures of the core complex of CBF3 alone and in association with a monomeric construct of Ndc10, using cryoelectron microscopy (cryo-EM). We identify the DNA-binding site of the complex and present a model in which CBF3 induces a tight bend in centromeric DNA, thus facilitating assembly of the centromeric nucleosome. PubMed: 30021170DOI: 10.1016/j.celrep.2018.06.068 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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