3HW7

High pressure (0.57 GPa) crystal structure of bovine copper, zinc superoxide dismutase at 2.0 angstroms

3HW7 の概要

• エントリーDOI: 10.2210/pdb3hw7/pdb
• 関連するPDBエントリー: 1cbj
• 分子名称: Superoxide dismutase [Cu-Zn], COPPER (I) ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: bovine, superoxide dismutase, high pressure, flexible electrostatic loop, antioxidant, disulfide bond, metal-binding, oxidoreductase, metal binding protein
• 由来する生物種: Bos taurus (bovine)
• 細胞内の位置: Cytoplasm: P00442
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31468.13

構造登録者

Ascone, I.,Savino, C. (登録日: 2009-06-17, 公開日: 2010-06-23, 最終更新日: 2024-11-20)

主引用文献

Ascone, I.,Savino, C.,Kahn, R.,Fourme, R.
Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa
Acta Crystallogr.,Sect.D, 66:654-663, 2010

PubMed Abstract: The 2 A resolution crystal structure of bovine erythrocyte Cu,Zn superoxide dismutase (CuZnSOD) has been determined by X-ray diffraction at high pressure (0.57 GPa) and room temperature. At 0.57 GPa the secondary, tertiary and quaternary structures are similar to other previously determined bovine erythrocyte CuZnSOD structures. Nevertheless, pressure has a localized impact on the atomic coordinates of C(alpha) atoms and on side chains. The compression of the crystal and of the protein backbone is anisotropic. This anisotropy is discussed, taking into account intermolecular contacts and protein conformation. Pressure perturbation highlights the more flexible zones in the protein such as the electrostatic loop. At 0.57 GPa, a global shift of the dimetallic sites in both subunits and changes in the oxidation state of Cu were observed. The flexibility of the electrostatic loop may be useful for the interaction of different metal carriers in the copper-uptake process, whereas the flexibility of the metal sites involved in the activity of the protein could contribute to explaining the ubiquitous character of CuZnSODs, which are found in organisms living in very different conditions, including the deep-sea environment. This work illustrates the potential of combining X-ray crystallography with high pressure to promote and stabilize higher energy conformational substates.

PubMed: 20516618
DOI: 10.1107/S0907444910012321

実験手法

X-RAY DIFFRACTION (2 Å)