9F2C
Archaeal histone protein HTkC from Thermococcus kodakarensis
9F2C の概要
エントリーDOI | 10.2210/pdb9f2c/pdb |
分子名称 | hypothetical protein (2 entities in total) |
機能のキーワード | archaeal histone, dna binding protein |
由来する生物種 | Thermococcus kodakarensis |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 27059.78 |
構造登録者 | |
主引用文献 | Schwab, S.,Hu, Y.,van Erp, B.,Cajili, M.K.M.,Hartmann, M.D.,Hernandez Alvarez, B.,Alva, V.,Boyle, A.L.,Dame, R.T. Histones and histone variant families in prokaryotes. Nat Commun, 15:7950-7950, 2024 Cited by PubMed Abstract: Histones are important chromatin-organizing proteins in eukaryotes and archaea. They form superhelical structures around which DNA is wrapped. Recent studies have shown that some archaea and bacteria contain alternative histones that exhibit different DNA binding properties, in addition to highly divergent sequences. However, the vast majority of these histones are identified in metagenomes and thus are difficult to study in vivo. The recent revolutionary breakthroughs in computational protein structure prediction by AlphaFold2 and RoseTTAfold allow for unprecedented insights into the potential function and structure of previously uncharacterized proteins. Here, we categorize the prokaryotic histone space into 17 distinct groups based on AlphaFold2 predictions. We identify a superfamily of histones, termed α3 histones, which are common in archaea and present in several bacteria. Importantly, we establish the existence of a large family of histones throughout archaea and in some bacteriophages that, instead of wrapping DNA, bridge DNA, thereby diverging from conventional nucleosomal histones. PubMed: 39261503DOI: 10.1038/s41467-024-52337-y 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.84 Å) |
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