Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/117906
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Type: Journal article
Title: The structure and activity of the glutathione reductase from Streptococcus pneumonia
Author: Sikanyika, M.
Aragão, D.
McDevitt, C.
Maher, M.
Citation: Acta Crystallographica Section F: Structural Biology Communications, 2019; 75(1):54-61
Publisher: International Union of Crystallography
Issue Date: 2019
ISSN: 2053-230X
2053-230X
Statement of
Responsibility: 
Mwilye Sikanyika, David Aragão, Christopher A. McDevitt and Megan J. Maher
Abstract: 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 comparisons with the interface structures of other GR enzymes, allows the classification of these enzymes into three classes. Analyses of the kinetic properties of SpGR revealed a significantly higher value for Km(GSSG) (231.2 ± 24.7 µM) in comparison to other characterized GR enzymes.
Keywords: Glutathione reductase; X-ray crystallography; Streptococcus pneumoniae
Rights: © 2019 International Union of Crystallography
RMID: 0030106533
DOI: 10.1107/S2053230X18016527
Appears in Collections:Microbiology and Immunology publications

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