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3MGP

Binding of Cobalt ions to the Nucleosome Core Particle

Summary for 3MGP
Entry DOI10.2210/pdb3mgp/pdb
Related1KX5 3MGQ 3MGR 3MGS
DescriptorHistone H3.2, Histone H4, Histone H2A, ... (8 entities in total)
Functional Keywordsprotein-dna complex, structural protein-dna complex, structural protein/dna
Biological sourceXenopus laevis (African clawed frog)
More
Total number of polymer chains10
Total formula weight200115.72
Authors
Mohideen, K.,Muhammad, R.,Davey, C.A. (deposition date: 2010-04-07, release date: 2010-06-16, Last modification date: 2023-11-01)
Primary citationMohideen, K.,Muhammad, R.,Davey, C.A.
Perturbations in nucleosome structure from heavy metal association.
Nucleic Acids Res., 38:6301-6311, 2010
Cited by
PubMed Abstract: Heavy metals have the potential to engage in strong bonding interactions and can thus function in essential as well as toxic or therapeutic capacities. We conducted crystallographic analyses of heavy cation binding to the nucleosome core particle and found that Co(2+) and Ni(2+) preferentially associate with the DNA major groove, in a sequence- and conformation-dependent manner. Conversely, Rb(+) and Cs(+) are found to bind only opportunistically to minor groove elements of the DNA, in particular at narrow AT dinucleotide sites. Furthermore, relative to Mn(2+) the aggressive coordination of Co(2+) and Ni(2+) to guanine bases is observed to induce a shift in histone-DNA register around the nucleosome center by stabilizing DNA stretching over one region accompanied by expulsion of two bases at an opposing location. These 'softer' transition metals also associate with multiple histone protein sites, including inter-nucleosomal cross-linking, and display a proclivity for coordination to histidine. Sustained binding and the ability to induce structural perturbations at specific locations in the nucleosome may contribute to genetic and epigenetic mechanisms of carcinogenesis mediated by Co(2+) and Ni(2+).
PubMed: 20494975
DOI: 10.1093/nar/gkq420
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.44 Å)
Structure validation

226707

건을2024-10-30부터공개중

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