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2BKY

Crystal structure of the Alba1:Alba2 heterodimer from sulfolobus solfataricus

Summary for 2BKY
Entry DOI10.2210/pdb2bky/pdb
Related1H0X 1H0Y 1UDV
DescriptorDNA/RNA-BINDING PROTEIN ALBA 1, DNA/RNA-BINDING PROTEIN ALBA 2, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
Functional Keywordsarchaeal dna binding protein, dna condensation, dna-binding, rna-binding, dna binding protein
Biological sourceSULFOLOBUS SOLFATARICUS
More
Cellular locationCytoplasm (Probable): P60849 Q97ZF4
Total number of polymer chains4
Total formula weight42305.52
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 citationJelinska, 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: 16004869
DOI: 10.1016/J.STR.2005.04.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

239492

數據於2025-07-30公開中

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