3B0B
Crystal structure of the chicken CENP-S/CENP-X complex
Summary for 3B0B
| Entry DOI | 10.2210/pdb3b0b/pdb |
| Related | 3B0C 3B0D |
| Descriptor | Centromere protein S, Centromere protein X (3 entities in total) |
| Functional Keywords | histone fold, dna binding, dna, nucleus, dna binding protein |
| Biological source | Gallus gallus More |
| Total number of polymer chains | 4 |
| Total formula weight | 42947.91 |
| 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) |
| 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 Cited by 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: 22304917DOI: 10.1016/j.cell.2011.11.061 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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