Structural highlights
Function[Q5IZD9_ACACA] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] Publication Abstract from PubMedThe iron superoxide dismutase found in the pathogenic amoeba Acanthamoeba castellanii (AcFeSOD) may play essential roles in the survival of the parasite, not only by protecting it from endogenous oxidative stress but also by detoxifying oxidative killing of the parasite by host immune effector cells. The AcFeSOD protein was expressed in a stable form using an Escherichia coli expression system and was crystallized by the microbatch and hanging-drop vapour-diffusion methods. The structure was determined to 2.33 A resolution from a single AcFeSOD crystal. The crystal belonged to the hexagonal space group P61 and contained 12 molecules forming three tetramers in the asymmetric unit, with an iron ion bound in each molecule. Structural comparisons and sequence alignment of AcFeSOD with other FeSODs showed a well conserved overall fold and conserved active-site residues with subtle differences. Crystal structure of an iron superoxide dismutase from the pathogenic amoeba Acanthamoeba castellanii.,Dao O, Asaithambi K, Na BK, Lee KH Acta Crystallogr F Struct Biol Commun. 2019 Jul 1;75(Pt 7):480-488. doi:, 10.1107/S2053230X19008112. Epub 2019 Jun 26. PMID:31282867[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 17:28, 20 November 2019.