The structure and activity of the glutathione reductase from Streptococcus pneumoniae
Mwilye Sikanyika, David Aragao, Christopher A McDevitt, Megan J Maher
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | INT UNION CRYSTALLOGRAPHY | Published : 2019
The glutathione reductase (GR) from Streptococcus pneumoniae is a flavoenzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH) in the cytoplasm of this bacterium. The maintenance of an intracellular pool of GSH is critical for the detoxification of reactive oxygen and nitrogen species and for intracellular metal tolerance to ions such as zinc. Here, S. pneumoniae GR (SpGR) was overexpressed and purified and its crystal structure determined at 2.56 Å resolution. SpGR shows overall structural similarity to other characterized GRs, with a dimeric structure that includes an antiparallel β-sheet at the dimer interface. This observation, in conjunction with com..View full abstract
Awarded by National Health and Medical Research Council of Australia
This work was funded by the National Health and Medical Research Council of Australia (GNT1080784 to MJM, DA and CAM). MS was funded by a La Trobe University Full Fee Research Scholarship (LTUFFRS).