Crystal Structure of the Yeast Inner Kinetochore Subunit cep3p
MetadataShow full item record
CitationBellizzi, John J. III, Peter K. Sorger, and Stephen C. Harrison. 2007. Crystal structure of the yeast inner kinetochore subunit cep3p. Structure 15(11): 1422-1430.
AbstractIn 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 Ctf13p-Skp1p heterodimer and contacts two sites on CDEIII. We report here the crystal structure, determined at 2.8 Å resolution by multiple isomorphous replacement with anomalous scattering, of a truncated Cep3p [Cep3p (47−608)], comprising all but an N-terminal, Zn2Cys6-cluster, DNAbinding module. Cep3p has a well-ordered structure throughout essentially all of its polypeptide chain, unlike most yeast transcription factors, including those with Zn2Cys6 clusters like Gal4p. This difference may reflect an underlying functional distinction: while 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 (47−603) and the known structures of Zn2Cys6 cluster domains, modeled the interaction of Cep3p with CDEIII.
Citable link to this pagehttp://nrs.harvard.edu/urn-3:HUL.InstRepos:3157878
- FAS Scholarly Articles