1H0Y
Structure of Alba: an archaeal chromatin protein modulated by acetylation
Summary for 1H0Y
| Entry DOI | 10.2210/pdb1h0y/pdb |
| Related | 1H0X |
| Descriptor | DNA BINDING PROTEIN SSO10B, SULFATE ION (3 entities in total) |
| Functional Keywords | archaea, chromatin, alba, acetylation, dna binding |
| Biological source | SULFOLOBUS SOLFATARICUS |
| Total number of polymer chains | 1 |
| Total formula weight | 11087.00 |
| Authors | Wardleworth, B.N.,Russell, R.J.M.,Bell, S.D.,Taylor, G.L.,White, M.F. (deposition date: 2002-07-01, release date: 2002-09-05, Last modification date: 2023-12-13) |
| Primary citation | Wardleworth, B.N.,Russell, R.J.M.,Bell, S.D.,Taylor, G.L.,White, M.F. Structure of Alba: An Archaeal Chromatin Protein Modulated by Acetylation Embo J., 21:4654-, 2002 Cited by PubMed Abstract: 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. PubMed: 12198167DOI: 10.1093/EMBOJ/CDF465 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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