5n56 | pdb_00005n56

Staphylococcus aureus Mn-dependent superoxide dismutase SodA

spinqualitylabelsall models 5n56, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n56 is a 2 chain structure with sequence from Staphylococcus aureus RF122. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.07Å Ligands: MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SODM1_STAAB Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Superoxide dismutase 3D structures

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