5N56

Staphylococcus aureus Mn-dependent superoxide dismutase SodA

Summary for 5N56

• Entry DOI: 10.2210/pdb5n56/pdb
• Descriptor: Superoxide dismutase [Mn/Fe] 1, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: superoxide dismutase, mn-dependent, staphylococcus aureus, oxidoreductase
• Biological source: Staphylococcus aureus (strain bovine RF122 / ET3-1)
• Total number of polymer chains: 2
• Total formula weight: 45586.47

Authors

Barwinska-Sendra, A.,Basle, A.,Waldron, K. (deposition date: 2017-02-13, release date: 2018-03-07, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.07 Å)