2BKY
Crystal structure of the Alba1:Alba2 heterodimer from sulfolobus solfataricus
Summary for 2BKY
Entry DOI | 10.2210/pdb2bky/pdb |
Related | 1H0X 1H0Y 1UDV |
Descriptor | DNA/RNA-BINDING PROTEIN ALBA 1, DNA/RNA-BINDING PROTEIN ALBA 2, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
Functional Keywords | archaeal dna binding protein, dna condensation, dna-binding, rna-binding, dna binding protein |
Biological source | SULFOLOBUS SOLFATARICUS More |
Cellular location | Cytoplasm (Probable): P60849 Q97ZF4 |
Total number of polymer chains | 4 |
Total formula weight | 42305.52 |
Authors | Jelinska, C.,Conroy, M.J.,Craven, C.J.,Bullough, P.A.,Waltho, J.P.,Taylor, G.L.,White, M.F. (deposition date: 2005-02-22, release date: 2005-07-14, Last modification date: 2024-05-08) |
Primary citation | Jelinska, C.,Conroy, M.J.,Craven, C.J.,Hounslow, A.M.,Bullough, P.A.,Waltho, J.P.,Taylor, G.L.,White, M.F. Obligate Heterodimerization of the Archaeal Alba2 Protein with Alba1 Provides a Mechanism for Control of DNA Packaging. Structure, 13:963-, 2005 Cited by PubMed Abstract: Organisms growing at elevated temperatures face a particular challenge to maintain the integrity of their genetic material. All thermophilic and hyperthermophilic archaea encode one or more copies of the Alba (Sac10b) gene. Alba is an abundant, dimeric, highly basic protein that binds cooperatively and at high density to DNA. Sulfolobus solfataricus encodes a second copy of the Alba gene, and the Alba2 protein is expressed at approximately 5% of the level of Alba1. We demonstrate by NMR, ITC, and crystallography that Alba2 exists exclusively as a heterodimer with Alba1 at physiological concentrations and that heterodimerization exerts a clear effect upon the DNA packaging, as observed by EM, potentially by changing the interface between adjacent Alba dimers in DNA complexes. A functional role for Alba2 in modulation of higher order chromatin structure and DNA condensation is suggested. PubMed: 16004869DOI: 10.1016/J.STR.2005.04.016 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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