1p3f
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| , resolution 2.90Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
OverviewOverview
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.
About this StructureAbout this Structure
1P3F is a Protein complex structure of sequences from Homo sapiens and Xenopus laevis. Full crystallographic information is available from OCA.
ReferenceReference
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
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