Structural highlights
5n57 is a 2 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Gene: | sodA, sodM, A4U86_04870, BN1321_40056, ERS072738_00830, ERS072840_00559, ERS073147_02394, ERS073767_02269, ERS074020_00889, ERS1058648_00955, FORC27_0128, HMPREF3211_00238, SAMEA2298760_02426 ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885) |
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[W8UU58_STAAU] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414]
Publication Abstract from PubMed
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 (1)H- and (14)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.
A charge polarization model for the metal-specific activity of superoxide dismutases.,Barwinska-Sendra A, Basle A, Waldron KJ, Un S Phys Chem Chem Phys. 2018 Jan 24;20(4):2363-2372. doi: 10.1039/c7cp06829h. PMID:29308487[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barwinska-Sendra A, Basle A, Waldron KJ, Un S. A charge polarization model for the metal-specific activity of superoxide dismutases. Phys Chem Chem Phys. 2018 Jan 24;20(4):2363-2372. doi: 10.1039/c7cp06829h. PMID:29308487 doi:http://dx.doi.org/10.1039/c7cp06829h
