2QUQ
Crystal Structure of the Essential Inner Kinetochore Protein Cep3p
Summary for 2QUQ
| Entry DOI | 10.2210/pdb2quq/pdb |
| Descriptor | Centromere DNA-binding protein complex CBF3 subunit B (2 entities in total) |
| Functional Keywords | dimer, centromere, chromosomal protein, dna-binding, metal-binding, nucleus, phosphorylation, zinc, protein binding, cell cycle, dna binding protein, structural protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus : P40969 |
| Total number of polymer chains | 1 |
| Total formula weight | 66094.52 |
| Authors | Bellizzi III, J.J.,Harrison, S.C. (deposition date: 2007-08-06, release date: 2007-11-13, Last modification date: 2024-02-21) |
| Primary citation | Bellizzi, J.J.,Sorger, P.K.,Harrison, S.C. Crystal structure of the yeast inner kinetochore subunit Cep3p. Structure, 15:1422-1430, 2007 Cited by PubMed Abstract: In budding yeast, the four-protein CBF3 complex (Skp1p-Ctf13p-Cep3p-Ndc10p) initiates kinetochore assembly by binding to the CDEIII locus of centromeric DNA. A Cep3p dimer recruits a Skp1p-Ctf13p heterodimer and contacts two sites on CDEIII. We report here the crystal structure, determined at 2.8 A resolution by multiple isomorphous replacement with anomalous scattering, of a truncated Cep3p (Cep3p [47-608]), comprising all but an N-terminal, Zn(2)Cys(6)-cluster, DNA-binding module. Cep3p has a well-ordered structure throughout essentially all of its polypeptide chain, unlike most yeast transcription factors, including those with Zn(2)Cys(6) clusters, such as Gal4p. This difference may reflect an underlying functional distinction: whereas any particular transcription factor must adapt to a variety of upstream activating sites, Cep3p scaffolds kinetochore assembly on centromeres uniformly configured on all 16 yeast chromosomes. We have, using the structure of Cep3p (47-608) and the known structures of Zn(2)Cys(6)-cluster domains, modeled the interaction of Cep3p with CDEIII. PubMed: 17997968DOI: 10.1016/j.str.2007.09.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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