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Structural Characterization of SOD4 from Candida albicans
Author(s) -
Randolph Keyera,
Galaleldeen Ahmad
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.913.12
Subject(s) - superoxide dismutase , candida albicans , reactive oxygen species , hydrogen peroxide , superoxide , chemistry , pathogen , innate immune system , microbiology and biotechnology , extracellular , biochemistry , yeast , sod1 , enzyme , fungus , biology , receptor , botany
Candida albicans is a fungal pathogen that infects immunocompromised individuals. During infection, the host's innate immune system responds by releasing reactive oxygen species (ROS) to fight off the invading microbes, however, the fungal pathogen is able to counter this response by releasing superoxide dismutase (SOD). SOD is an enzyme that catalyzes dismutation of superoxide radicals into hydrogen peroxide and molecular oxygen. There are several fungal SODs that play a vital role in defending the fungus against ROS such as Cu/Zn SOD (SOD1), SOD4, SOD5 and SOD6. The structure of SOD5 has been recently determined. It is similar to the dimeric SOD1 in that it maintains the beta‐barrel and the copper binding, but it lacks both the zinc‐binding site and the electrostatic loop, and it is monomeric. SOD4 is homologous to SOD5 and is predicted to be extracellular. SOD4 was overexpressed, and since SOD4 is insoluble, the protein was denatured, refolded and purified. Crystallization trials are underway in pursuit of the SOD4 structure.