5N57

Staphylococcus aureus cambialistic superoxide dismutase SodM

5N57 の概要

• エントリーDOI: 10.2210/pdb5n57/pdb
• 分子名称: Superoxide dismutase, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: superoxide dismutase, cambialistic, staphylococcus aureus, oxidoreductase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46245.62

構造登録者

Barwinska-Sendra, A.,Basle, A.,Waldron, K. (登録日: 2017-02-13, 公開日: 2018-03-07, 最終更新日: 2024-01-17)

主引用文献

Barwinska-Sendra, A.,Basle, A.,Waldron, K.J.,Un, S.
A charge polarization model for the metal-specific activity of superoxide dismutases.
Phys Chem Chem Phys, 20:2363-2372, 2018

PubMed Abstract: The pathogenicity of Staphylococcus aureus is enhanced by having two superoxide dismutases (SODs): a Mn-specific SOD and another that can use either Mn or Fe. Using 94 GHz electron-nuclear double resonance (ENDOR) and electron double resonance detected (ELDOR)-NMR we show that, despite their different metal-specificities, their structural and electronic similarities extend down to their active-site H- and N-Mn(ii) hyperfine interactions. However these interactions, and hence the positions of these nuclei, are different in the inactive Mn-reconstituted Escherichia coli Fe-specific SOD. Density functional theory modelling attributes this to a different angular position of the E. coli H171 ligand. This likely disrupts the Mn-H171-E170' triad causing a shift in charge and in metal redox potential, leading to the loss of activity. This is supported by the correlated differences in the Mn(ii) zero-field interactions of the three SOD types and suggests that the triad is important for determining metal specific activity.

PubMed: 29308487
DOI: 10.1039/c7cp06829h

実験手法

X-RAY DIFFRACTION (2.3 Å)