1h0y
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Eukaryotic DNA is packaged into nucleosomes that regulate the, accessibility of the genome to replication, transcription and repair, factors. Chromatin accessibility is controlled by histone modifications, including acetylation and methylation. Archaea possess eukary otic-like, machineries for DNA replication, transcription and information processing., The conserved archaeal DNA binding protein Alba (formerly Sso10b), interacts with the silencing protein Sir2, which regulates Alba's DNA, binding affinity by deacetylation of a lysine residue. We present the, crystal structure of Alba from Sulfolobus solfataricus at 2.6 A resolution, (PDB code 1h0x). The fold is reminiscent of the N-terminal DNA binding, domain of DNase I and the C-terminal domain of initiation factor IF3. The, Alba dimer ... | + | Eukaryotic DNA is packaged into nucleosomes that regulate the, accessibility of the genome to replication, transcription and repair, factors. Chromatin accessibility is controlled by histone modifications, including acetylation and methylation. Archaea possess eukary otic-like, machineries for DNA replication, transcription and information processing., The conserved archaeal DNA binding protein Alba (formerly Sso10b), interacts with the silencing protein Sir2, which regulates Alba's DNA, binding affinity by deacetylation of a lysine residue. We present the, crystal structure of Alba from Sulfolobus solfataricus at 2.6 A resolution, (PDB code 1h0x). The fold is reminiscent of the N-terminal DNA binding, domain of DNase I and the C-terminal domain of initiation factor IF3. The, Alba dimer has two extended beta-hairpins flanking a central body, containing the acetylated lysine, Lys16, suggesting three main points of, contact with the DNA. Fluorescence, calorimetry and electrophoresis data, suggest a final binding stoichiometry of approximately 5 bp DNA per Alba, dimer. We present a model for the Alba-DNA interaction consistent with the, available structural, biophysical and electron microscopy data. |
==About this Structure== | ==About this Structure== | ||
| - | 1H0Y is a | + | 1H0Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: SO4. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H0Y OCA]. |
==Reference== | ==Reference== | ||
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[[Category: dna binding]] | [[Category: dna binding]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:34:46 2007'' |
Revision as of 11:29, 5 November 2007
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STRUCTURE OF ALBA: AN ARCHAEAL CHROMATIN PROTEIN MODULATED BY ACETYLATION
Overview
Eukaryotic DNA is packaged into nucleosomes that regulate the, accessibility of the genome to replication, transcription and repair, factors. Chromatin accessibility is controlled by histone modifications, including acetylation and methylation. Archaea possess eukary otic-like, machineries for DNA replication, transcription and information processing., The conserved archaeal DNA binding protein Alba (formerly Sso10b), interacts with the silencing protein Sir2, which regulates Alba's DNA, binding affinity by deacetylation of a lysine residue. We present the, crystal structure of Alba from Sulfolobus solfataricus at 2.6 A resolution, (PDB code 1h0x). The fold is reminiscent of the N-terminal DNA binding, domain of DNase I and the C-terminal domain of initiation factor IF3. The, Alba dimer has two extended beta-hairpins flanking a central body, containing the acetylated lysine, Lys16, suggesting three main points of, contact with the DNA. Fluorescence, calorimetry and electrophoresis data, suggest a final binding stoichiometry of approximately 5 bp DNA per Alba, dimer. We present a model for the Alba-DNA interaction consistent with the, available structural, biophysical and electron microscopy data.
About this Structure
1H0Y is a Single protein structure of sequence from Sulfolobus solfataricus with SO4 as ligand. Structure known Active Site: SO4. Full crystallographic information is available from OCA.
Reference
Structure of Alba: an archaeal chromatin protein modulated by acetylation., Wardleworth BN, Russell RJ, Bell SD, Taylor GL, White MF, EMBO J. 2002 Sep 2;21(17):4654-62. PMID:12198167
Page seeded by OCA on Mon Nov 5 13:34:46 2007
