2PYO

Drosophila nucleosome core

Summary for 2PYO

• Entry DOI: 10.2210/pdb2pyo/pdb
• Descriptor: DNA (147-MER), Histone H3, Histone H4, ... (9 entities in total)
• Functional Keywords: nucleosome core, histone fold, structural protein-dna complex, structural protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus (By similarity): 2PYO; Nucleus: 2PYO P02299 P84040
• Total number of polymer chains: 10
• Total formula weight: 197820.27

Authors

Clapier, C.R.,Petosa, C.,Mueller, C.W. (deposition date: 2007-05-16, release date: 2007-11-06, Last modification date: 2024-02-21)

Primary citation

Clapier, C.R.,Chakravarthy, S.,Petosa, C.,Fernandez-Tornero, C.,Luger, K.,Muller, C.W.
Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer.
Proteins, 71:1-7, 2007

PubMed Abstract: We determined the 2.45 A crystal structure of the nucleosome core particle from Drosophila melanogaster and compared it to that of Xenopus laevis bound to the identical 147 base-pair DNA fragment derived from human alpha-satellite DNA. Differences between the two structures primarily reflect 16 amino acid substitutions between species, 15 of which are in histones H2A and H2B. Four of these involve histone tail residues, resulting in subtly altered protein-DNA interactions that exemplify the structural plasticity of these tails. Of the 12 substitutions occurring within the histone core regions, five involve small, solvent-exposed residues not involved in intraparticle interactions. The remaining seven involve buried hydrophobic residues, and appear to have coevolved so as to preserve the volume of side chains within the H2A hydrophobic core and H2A-H2B dimer interface. Thus, apart from variations in the histone tails, amino acid substitutions that differentiate Drosophila from Xenopus histones occur in mutually compensatory combinations. This highlights the tight evolutionary constraints exerted on histones since the vertebrate and invertebrate lineages diverged.

PubMed: 17957772
DOI: 10.1002/prot.21720

Experimental method

X-RAY DIFFRACTION (2.43 Å)