2cv5
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Crystal structure of human nucleosome core particle
OverviewOverview
Gene expression in eukaryotes depends upon positioning, mobility and, packaging of nucleosomes; thus, we need the detailed information of the, human nucleosome core particle (NCP) structure, which could clarify, chromatin properties. Here, we report the 2.5 A crystal structure of a, human NCP. The overall structure is similar to those of other NCPs, reported previously. However, the DNA path of human NCP is remarkably, different from that taken within other NCPs with an identical DNA, sequence. A comparison of the structural parameters between human and, Xenopus laevis DNA reveals that the DNA path of human NCP consecutively, shifts by 1 bp in the regions of superhelix axis location -5.0 to -2.0 and, 5.0 to 7.0. This alteration of the human DNA path is caused predominantly, by tight DNA-DNA contacts within the crystal. It is also likely that the, conformational change in the human H2B tail induces the local alteration, of the DNA path. In human NCP, the region with the altered DNA path lacks, Mn2+ ions and the B-factors of the DNA phosphate groups are substantially, high. Therefore, in contrast to the histone octamer, the nucleosomal DNA, is sufficiently flexible and mobile and can undergo drastic conformational, changes, depending upon the environment.
About this StructureAbout this Structure
2CV5 is a Protein complex structure of sequences from Homo sapiens with MN and CL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle., Tsunaka Y, Kajimura N, Tate S, Morikawa K, Nucleic Acids Res. 2005 Jun 10;33(10):3424-34. Print 2005. PMID:15951514
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