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3UT9

Crystal Structure of Nucleosome Core Particle Assembled with a Palindromic Widom '601' Derivative (NCP-601L)

Summary for 3UT9
Entry DOI10.2210/pdb3ut9/pdb
DescriptorHistone H3.2, Histone H4, Histone H2A, ... (10 entities in total)
Functional Keywordsnucleosome core particle, ncp, 601-sequence dna, structural protein-dna complex, structural protein/dna
Biological sourceXenopus laevis (African clawed frog)
More
Cellular locationNucleus: P84233 P62799 P02281
Nucleus (By similarity): Q6AZJ8
Total number of polymer chains10
Total formula weight200043.33
Authors
Chua, E.Y.D.,Vasudevan, D.,Davey, G.E.,Wu, B.,Davey, C.A. (deposition date: 2011-11-25, release date: 2012-04-11, Last modification date: 2024-03-20)
Primary citationChua, E.Y.D.,Vasudevan, D.,Davey, G.E.,Wu, B.,Davey, C.A.
The mechanics behind DNA sequence-dependent properties of the nucleosome
Nucleic Acids Res., 40:6338-6352, 2012
Cited by
PubMed Abstract: Chromatin organization and composition impart sophisticated regulatory features critical to eukaryotic genomic function. Although DNA sequence-dependent histone octamer binding is important for nucleosome activity, many aspects of this phenomenon have remained elusive. We studied nucleosome structure and stability with diverse DNA sequences, including Widom 601 derivatives with the highest known octamer affinities, to establish a simple model behind the mechanics of sequence dependency. This uncovers the unique but unexpected role of TA dinucleotides and a propensity for G|C-rich sequence elements to conform energetically favourably at most locations around the histone octamer, which rationalizes G|C% as the most predictive factor for nucleosome occupancy in vivo. In addition, our findings reveal dominant constraints on double helix conformation by H3-H4 relative to H2A-H2B binding and DNA sequence context-dependency underlying nucleosome structure, positioning and stability. This provides a basis for improved prediction of nucleosomal properties and the design of tailored DNA constructs for chromatin investigations.
PubMed: 22453276
DOI: 10.1093/nar/gks261
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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