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5B2J

Human nucleosome containing CpG methylated DNA

Summary for 5B2J
Entry DOI10.2210/pdb5b2j/pdb
Related5B2I
DescriptorHistone H3.1, Histone H4, Histone H2A type 1-B/E, ... (7 entities in total)
Functional Keywordschromatin, epigenetics, histone, transcription, transcription-dna complex, transcription/dna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains10
Total formula weight202725.49
Authors
Fujii, Y.,Wakamori, M.,Umehara, T.,Yokoyama, S. (deposition date: 2016-01-18, release date: 2016-06-15, Last modification date: 2023-11-08)
Primary citationFujii, Y.,Wakamori, M.,Umehara, T.,Yokoyama, S.
Crystal structure of human nucleosome core particle containing enzymatically introduced CpG methylation.
Febs Open Bio, 6:498-514, 2016
Cited by
PubMed Abstract: Cytosine methylation, predominantly of the CpG sequence in vertebrates, is one of the major epigenetic modifications crucially involved in the control of gene expression. Due to the difficulty of reconstituting site-specifically methylated nucleosomal DNA at crystallization quality, most structural analyses of CpG methylation have been performed using chemically synthesized oligonucleotides, There has been just one recent study of nucleosome core particles (NCPs) reconstituted with nonpalindromic human satellite 2-derived DNAs. Through the preparation of a 146-bp palindromic α-satellite-based nucleosomal DNA containing four CpG dinucleotide sequences and its enzymatic methylation and restriction, we reconstituted a 'symmetric' human CpG-methylated nucleosome core particle (NCP). We solved the crystal structures of the CpG-methylated and unmodified NCPs at 2.6 and 3.0 Å resolution, respectively. We observed the electron densities of two methyl groups, among the eight 5-methylcytosines introduced in the CpG-fully methylated NCP. There were no obvious structural differences between the CpG-methylated 'symmetric NCP' and the unmodified NCP. The preparation of a crystallization-grade CpG-methylated NCP provides a platform for the analysis of CpG-methyl reader and eraser proteins.
PubMed: 27419055
DOI: 10.1002/2211-5463.12064
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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