3MGP

Binding of Cobalt ions to the Nucleosome Core Particle

3MGP の概要

• エントリーDOI: 10.2210/pdb3mgp/pdb
• 関連するPDBエントリー: 1KX5 3MGQ 3MGR 3MGS
• 分子名称: Histone H3.2, Histone H4, Histone H2A, ... (8 entities in total)
• 機能のキーワード: protein-dna complex, structural protein-dna complex, structural protein/dna
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 200115.72

構造登録者

Mohideen, K.,Muhammad, R.,Davey, C.A. (登録日: 2010-04-07, 公開日: 2010-06-16, 最終更新日: 2023-11-01)

主引用文献

Mohideen, K.,Muhammad, R.,Davey, C.A.
Perturbations in nucleosome structure from heavy metal association.
Nucleic Acids Res., 38:6301-6311, 2010

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

実験手法

X-RAY DIFFRACTION (2.44 Å)