1ID3

CRYSTAL STRUCTURE OF THE YEAST NUCLEOSOME CORE PARTICLE REVEALS FUNDAMENTAL DIFFERENCES IN INTER-NUCLEOSOME INTERACTIONS

Summary for 1ID3

• Entry DOI: 10.2210/pdb1id3/pdb
• Related: 1AOI 1EQZ 1F66
• Descriptor: PALINDROMIC 146BP DNA FRAGMENT, HISTONE H3, HISTONE H4, ... (7 entities in total)
• Functional Keywords: nucleosome core particle, chromatin, histone, protein/dna interaction, nucleoprotein, supercoiled dna, complex (nucleosome core-dna), structural protein-dna complex, structural protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P61830 P02309 P04911 P02294
• Total number of polymer chains: 10
• Total formula weight: 200149.94

Authors

White, C.L.,Suto, R.K.,Luger, K. (deposition date: 2001-04-03, release date: 2001-09-28, Last modification date: 2023-08-09)

Primary citation

White, C.L.,Suto, R.K.,Luger, K.
Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions.
EMBO J., 20:5207-5218, 2001

PubMed Abstract: Chromatin is composed of nucleosomes, the universally repeating protein-DNA complex in eukaryotic cells. The crystal structure of the nucleosome core particle from Saccharomyces cerevisiae reveals that the structure and function of this fundamental complex is conserved between single-cell organisms and metazoans. Our results show that yeast nucleosomes are likely to be subtly destabilized as compared with nucleosomes from higher eukaryotes, consistent with the idea that much of the yeast genome remains constitutively open during much of its life cycle. Importantly, minor sequence variations lead to dramatic changes in the way in which nucleosomes pack against each other within the crystal lattice. This has important implications for our understanding of the formation of higher order chromatin structure and its modulation by post-translational modifications. Finally, the yeast nucleosome core particle provides a structural context by which to interpret genetic data obtained from yeast. Coordinates have been deposited with the Protein Data Bank under accession number 1ID3.

PubMed: 11566884
DOI: 10.1093/emboj/20.18.5207

Experimental method

X-RAY DIFFRACTION (3.1 Å)