6F07
CBF3 Core Complex
Summary for 6F07
| Entry DOI | 10.2210/pdb6f07/pdb |
| EMDB information | 4163 |
| Descriptor | Centromere DNA-binding protein complex CBF3 subunit B, Suppressor of kinetochore protein 1, ZINC ION (3 entities in total) |
| Functional Keywords | kinetochore, f-box, dna-binding, centromere, cell cycle |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 3 |
| Total formula weight | 167762.32 |
| Authors | Leber, V.,Singleton, M.R. (deposition date: 2017-11-17, release date: 2017-12-13, Last modification date: 2024-10-09) |
| Primary citation | Leber, V.,Nans, A.,Singleton, M.R. Structural basis for assembly of the CBF3 kinetochore complex. EMBO J., 37:269-281, 2018 Cited by PubMed Abstract: Eukaryotic chromosomes contain a specialised region known as the centromere, which forms the platform for kinetochore assembly and microtubule attachment. The centromere is distinguished by the presence of nucleosomes containing the histone H3 variant, CENP-A. In budding yeast, centromere establishment begins with the recognition of a specific DNA sequence by the CBF3 complex. This in turn facilitates CENP-A nucleosome deposition and kinetochore assembly. Here, we describe a 3.6 Å single-particle cryo-EM reconstruction of the core CBF3 complex, incorporating the sequence-specific DNA-binding protein Cep3 together with regulatory subunits Ctf13 and Skp1. This provides the first structural data on Ctf13, defining it as an F-box protein of the leucine-rich-repeat family, and demonstrates how a novel F-box-mediated interaction between Ctf13 and Skp1 is responsible for initial assembly of the CBF3 complex. PubMed: 29212814DOI: 10.15252/embj.201798134 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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