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1h0y
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Revision as of 13:20, 30 October 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 ... [(full description)]
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
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