1h0x
From Proteopedia
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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
1H0X is a Single protein structure of sequence from Sulfolobus solfataricus. 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
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