2QUQ

Crystal Structure of the Essential Inner Kinetochore Protein Cep3p

2QUQ の概要

• エントリーDOI: 10.2210/pdb2quq/pdb
• 分子名称: Centromere DNA-binding protein complex CBF3 subunit B (2 entities in total)
• 機能のキーワード: dimer, centromere, chromosomal protein, dna-binding, metal-binding, nucleus, phosphorylation, zinc, protein binding, cell cycle, dna binding protein, structural protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus : P40969
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 66094.52

構造登録者

Bellizzi III, J.J.,Harrison, S.C. (登録日: 2007-08-06, 公開日: 2007-11-13, 最終更新日: 2024-02-21)

主引用文献

Bellizzi, J.J.,Sorger, P.K.,Harrison, S.C.
Crystal structure of the yeast inner kinetochore subunit Cep3p.
Structure, 15:1422-1430, 2007

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: 17997968
DOI: 10.1016/j.str.2007.09.008

実験手法

X-RAY DIFFRACTION (2.8 Å)