2VEQ
Insights into kinetochore-DNA interactions from the structure of Cep3p
Summary for 2VEQ
| Entry DOI | 10.2210/pdb2veq/pdb |
| Descriptor | CENTROMERE DNA-BINDING PROTEIN COMPLEX CBF3 SUBUNIT B, BETA-MERCAPTOETHANOL, CACODYLATE ION, ... (4 entities in total) |
| Functional Keywords | transcription factor, cell cycle, zinc, cep3p, nucleus, centromere, dna-binding, phosphorylation, chromosomal protein, kinetochore, cbf3 complex, metal-binding |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Cellular location | Nucleus : P40969 |
| Total number of polymer chains | 1 |
| Total formula weight | 66593.94 |
| Authors | Purvis, A.,Singleton, M.R. (deposition date: 2007-10-26, release date: 2007-12-25, Last modification date: 2017-07-12) |
| Primary citation | Purvis, A.,Singleton, M.R. Insights Into Kinetochore-DNA Interactions from the Structure of Cep3Delta Embo Rep., 9:56-, 2008 Cited by PubMed Abstract: The CBF3 complex is an essential core component of the budding yeast kinetochore and is required for the centromeric localization of all other kinetochore proteins. We determined the crystal structure of a large section of the protein Cep3 from CBF3, which is the only component with obvious DNA-binding motifs. The protein adopts a roughly bilobal shape, with an extended dimerization interface. The dimer has a large central channel that is sufficient to accommodate duplex B-form DNA. The zinc-finger domains emerge at the edges of the channel, and could bind to the DNA in a pseudo-symmetrical manner at degenerate half-sites in the centromeric sequence. We propose a mechanism for the modulation of DNA affinity by an acidic activator domain, which could be applicable to a wider family of transcription factors. PubMed: 18064045DOI: 10.1038/SJ.EMBOR.7401139 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
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