Crystal Structure of the Yeast Inner Kinetochore Subunit cep3p
| Title: | Crystal Structure of the Yeast Inner Kinetochore Subunit cep3p |
| Author: |
Sorger, Peter; Bellizzi, John J. III; Harrison, Stephen
Note: Order does not necessarily reflect citation order of authors. |
| Citation: | Bellizzi, 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. |
| Full Text & Related Files: |
Harrison_Crystal Structure.pdf (5.203Mb; PDF) 
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| 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 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. |
| Published Version: | http://dx.doi.org/10.1016/j.str.2007.09.008 |
| Other Sources: | http://crystal.harvard.edu/publications.php |
| Terms of Use: | This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA |
| Citable link to this page: | http://nrs.harvard.edu/urn-3:HUL.InstRepos:3157878 |
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