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| '''Drosophila nucleosome core'''
| | ===Drosophila nucleosome core=== |
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| ==Overview==
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| 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. Proteins 2008. (c) 2007 Wiley-Liss, Inc.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17957772}}, adds the Publication Abstract to the page |
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| | {{ABSTRACT_PUBMED_17957772}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nucleosome core]] | | [[Category: Nucleosome core]] |
| [[Category: Structural protein/dna complex]] | | [[Category: Structural protein/dna complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:01:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:24:10 2008'' |
