3B0C

Crystal structure of the chicken CENP-T histone fold/CENP-W complex, crystal form I

Summary for 3B0C

• Entry DOI: 10.2210/pdb3b0c/pdb
• Related: 3B0B 3B0D
• Descriptor: Centromere protein T, Centromere protein W, CITRIC ACID, ... (4 entities in total)
• Functional Keywords: histone fold, dna binding, dna binding protein
• Biological source: Gallus gallus (chickens); More
• Total number of polymer chains: 2
• Total formula weight: 22015.71

Authors

Nishino, T.,Takeuchi, K.,Gascoigne, K.E.,Suzuki, A.,Hori, T.,Oyama, T.,Morikawa, K.,Cheeseman, I.M.,Fukagawa, T. (deposition date: 2011-06-08, release date: 2012-03-07, Last modification date: 2024-03-13)

Primary citation

Nishino, T.,Takeuchi, K.,Gascoigne, K.E.,Suzuki, A.,Hori, T.,Oyama, T.,Morikawa, K.,Cheeseman, I.M.,Fukagawa, T.
CENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Fold.
Cell(Cambridge,Mass.), 148:487-501, 2012

PubMed Abstract: The multiprotein kinetochore complex must assemble at a specific site on each chromosome to achieve accurate chromosome segregation. Defining the nature of the DNA-protein interactions that specify the position of the kinetochore and provide a scaffold for kinetochore formation remain key goals. Here, we demonstrate that the centromeric histone-fold-containing CENP-T-W and CENP-S-X complexes coassemble to form a stable CENP-T-W-S-X heterotetramer. High-resolution structural analysis of the individual complexes and the heterotetramer reveals similarity to other histone fold-containing complexes including canonical histones within a nucleosome. The CENP-T-W-S-X heterotetramer binds to and supercoils DNA. Mutants designed to compromise heterotetramerization or the DNA-protein contacts around the heterotetramer strongly reduce the DNA binding and supercoiling activities in vitro and compromise kinetochore assembly in vivo. These data suggest that the CENP-T-W-S-X complex forms a unique nucleosome-like structure to generate contacts with DNA, extending the "histone code" beyond canonical nucleosome proteins.

PubMed: 22304917
DOI: 10.1016/j.cell.2011.11.061

Experimental method

X-RAY DIFFRACTION (2.201 Å)