3RN4

Crystal structure of iron-substituted Sod2 from Saccharomyces cerevisiae

3RN4 の概要

• エントリーDOI: 10.2210/pdb3rn4/pdb
• 関連するPDBエントリー: 3BFR
• 分子名称: Superoxide dismutase [Mn], mitochondrial, FE (III) ION (3 entities in total)
• 機能のキーワード: mitochondrial manganese superoxide dismutase, iron-binding, mitochondrion, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Mitochondrion matrix: P00447
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24052.80

構造登録者

Kang, Y.,He, Y.-X.,Cheng, W.,Zhou, C.-Z.,Li, W.-F. (登録日: 2011-04-21, 公開日: 2011-11-23, 最終更新日: 2023-11-01)

主引用文献

Kang, Y.,He, Y.-X.,Zhao, M.-X.,Li, W.-F.
Structures of native and Fe-substituted SOD2 from Saccharomyces cerevisiae
Acta Crystallogr.,Sect.F, 67:1173-1178, 2011

PubMed Abstract: The manganese-specific superoxide dismutase SOD2 from the yeast Saccharomyces cerevisiae is a protein that resides in the mitochondrion and protects it against attack by superoxide radicals. However, a high iron concentration in the mitochondria results in iron misincorporation at the active site, with subsequent inactivation of SOD2. Here, the crystal structures of SOD2 bound with the native metal manganese and with the `wrong' metal iron are presented at 2.05 and 1.79 Å resolution, respectively. Structural comparison of the two structures shows no significant conformational alteration in the overall structure or in the active site upon binding the non-native metal iron. Moreover, residues Asp163 and Lys80 are proposed to potentially be responsible for the metal specificity of the Mn-specific SOD. Additionally, the surface-potential distribution of SOD2 revealed a conserved positively charged electrostatic zone in the proximity of the active site that probably functions in the same way as in Cu/Zn-SODs by facilitating the diffusion of the superoxide anion to the metal ion.

PubMed: 22102021
DOI: 10.1107/S1744309111029186

実験手法

X-RAY DIFFRACTION (1.79 Å)