2h9u
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Eukaryotic DNA is packaged into nucleosomes that regulate the | + | 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== | ||
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[[Category: Aeropyrum pernix]] | [[Category: Aeropyrum pernix]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kumarevel, T | + | [[Category: Kumarevel, T S.]] |
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sakamoto, K.]] | [[Category: Sakamoto, K.]] | ||
[[Category: Shinkai, A.]] | [[Category: Shinkai, A.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:39:39 2008'' |
Revision as of 15:39, 21 February 2008
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Crystal structure of the archaea specific DNA binding protein
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
2H9U is a Single protein structure of sequence from Aeropyrum pernix with as ligand. 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 Thu Feb 21 17:39:39 2008
Categories: Aeropyrum pernix | Single protein | Kumarevel, T S. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sakamoto, K. | Shinkai, A. | Yokoyama, S. | EDO | Archaea | Crystal structure | Dna binding protein | National project on protein structural and functional analyses | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
