Structural highlights
1p3f is a 10 chain structure with sequence from [1] and African clawed frog. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Related: | 1aoi, 1f66, 1id3, 1kx3, 1kx4, 1kx5, 1p34, 1p3a, 1p3b, 1p3g, 1p3i, 1p3k, 1p3l, 1p3m, 1p3o, 1p3p |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[H4_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [H2B11_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Here we describe 11 crystal structures of nucleosome core particles containing individual point mutations in the structured regions of histones H3 and H4. The mutated residues are located at the two protein-DNA interfaces flanking the nucleosomal dyad. Five of the mutations partially restore the in vivo effects of SWI/SNF inactivation in yeast. We find that even nonconservative mutations of these residues (which exhibit a distinct phenotype in vivo) have only moderate effects on global nucleosome structure. Rather, local protein-DNA interactions are disrupted and weakened in a subtle and complex manner. The number of lost protein-DNA interactions correlates directly with an increased propensity of the histone octamer to reposition with respect to the DNA, and with an overall destabilization of the nucleosome. Thus, the disruption of only two to six of the approximately 120 direct histone-DNA interactions within the nucleosome has a pronounced effect on nucleosome mobility and stability. This has implications for our understanding of how these structures are made accessible to the transcription and replication machinery in vivo.
Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions.,Muthurajan UM, Bao Y, Forsberg LJ, Edayathumangalam RS, Dyer PN, White CL, Luger K EMBO J. 2004 Jan 28;23(2):260-71. Epub 2004 Jan 22. PMID:14739929[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Muthurajan UM, Bao Y, Forsberg LJ, Edayathumangalam RS, Dyer PN, White CL, Luger K. Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions. EMBO J. 2004 Jan 28;23(2):260-71. Epub 2004 Jan 22. PMID:14739929 doi:http://dx.doi.org/10.1038/sj.emboj.7600046
