2pyo: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2PYO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PYO OCA]. | 2PYO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Mn+Binding+Site+For+Residue+E+1002'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Residue+J+1003'>AC2</scene>, <scene name='pdbsite=AC3:Mn+Binding+Site+For+Residue+J+1009'>AC3</scene>, <scene name='pdbsite=AC4:Mn+Binding+Site+For+Residue+I+1011'>AC4</scene>, <scene name='pdbsite=AC5:Mn+Binding+Site+For+Residue+I+1012'>AC5</scene>, <scene name='pdbsite=AC6:Mn+Binding+Site+For+Residue+I+1013'>AC6</scene>, <scene name='pdbsite=AC7:Mn+Binding+Site+For+Residue+J+1014'>AC7</scene>, <scene name='pdbsite=AC8:Cl+Binding+Site+For+Residue+H+1015'>AC8</scene>, <scene name='pdbsite=AC9:Cl+Binding+Site+For+Residue+D+1016'>AC9</scene>, <scene name='pdbsite=BC1:Cl+Binding+Site+For+Residue+A+1017'>BC1</scene> and <scene name='pdbsite=BC2:Cl+Binding+Site+For+Residue+E+1018'>BC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PYO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: structural protein/dna complex]] | [[Category: structural protein/dna complex]] | ||
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Revision as of 14:25, 5 March 2008
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Drosophila nucleosome core
OverviewOverview
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.
About this StructureAbout this Structure
2PYO is a Protein complex structure of sequences from Drosophila melanogaster and Homo sapiens with and as ligands. Known structural/functional Sites: , , , , , , , , , and . Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer., Clapier CR, Chakravarthy S, Petosa C, Fernandez-Tornero C, Luger K, Muller CW, Proteins. 2007 Oct 23;71(1):1-7. PMID:17957772
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