6qv8
Staphylococcus aureus superoxide dismutase SodM double mutantStaphylococcus aureus superoxide dismutase SodM double mutant
Structural highlights
FunctionSODM2_STAA8 Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal ion at the active site. May play a role in maintaining cell viability during the late-exponential and stationary phases of growth since it becomes a major source of activity under oxidative stress. Has a role in resisting external superoxide stress. Involved in acid tolerance and the acid-adaptive response. Mediates the derepression of perR regulon in the response to HOCl stress at low level of SOD activity (By similarity).[1] [2] Publication Abstract from PubMedAlmost half of all enzymes utilize a metal cofactor. However, the features that dictate the metal utilized by metalloenzymes are poorly understood, limiting our ability to manipulate these enzymes for industrial and health-associated applications. The ubiquitous iron/manganese superoxide dismutase (SOD) family exemplifies this deficit, as the specific metal used by any family member cannot be predicted. Biochemical, structural and paramagnetic analysis of two evolutionarily related SODs with different metal specificity produced by the pathogenic bacterium Staphylococcus aureus identifies two positions that control metal specificity. These residues make no direct contacts with the metal-coordinating ligands but control the metal's redox properties, demonstrating that subtle architectural changes can dramatically alter metal utilization. Introducing these mutations into S. aureus alters the ability of the bacterium to resist superoxide stress when metal starved by the host, revealing that small changes in metal-dependent activity can drive the evolution of metalloenzymes with new cofactor specificity. An evolutionary path to altered cofactor specificity in a metalloenzyme.,Barwinska-Sendra A, Garcia YM, Sendra KM, Basle A, Mackenzie ES, Tarrant E, Card P, Tabares LC, Bicep C, Un S, Kehl-Fie TE, Waldron KJ Nat Commun. 2020 Jun 1;11(1):2738. doi: 10.1038/s41467-020-16478-0. PMID:32483131[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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