Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins

Daniel Trnka, Anna D. Engelke, Manuela Gellert, Anna Moseler, Md Faruq Hossain, Tobias T. Lindenberg, Luca Pedroletti, Benjamin Odermatt, João V. Souza, Agnieszka K. Bronowska, Tobias P. Dick, Uli Mühlenhoff, Andreas J. Meyer, Carsten Berndt and Christopher Horst Lillig ()
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Daniel Trnka: Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald
Anna D. Engelke: Medical Faculty, Heinrich-Heine University Düsseldorf
Manuela Gellert: Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald
Anna Moseler: Institute of Crop Science and Resource Conservation, University of Bonn
Md Faruq Hossain: Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald
Tobias T. Lindenberg: Institute of Neuroanatomy, University Clinics, University of Bonn
Luca Pedroletti: Institute of Crop Science and Resource Conservation, University of Bonn
Benjamin Odermatt: Institute of Neuroanatomy, University Clinics, University of Bonn
João V. Souza: Chemistry, School of Natural and Environmental Sciences, Newcastle University
Agnieszka K. Bronowska: Chemistry, School of Natural and Environmental Sciences, Newcastle University
Tobias P. Dick: Division of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ)
Uli Mühlenhoff: Institute for Cytobiology and Cytopathology, Philipps University Marburg
Andreas J. Meyer: Institute of Crop Science and Resource Conservation, University of Bonn
Carsten Berndt: Medical Faculty, Heinrich-Heine University Düsseldorf
Christopher Horst Lillig: Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: Abstract Despite their very close structural similarity, CxxC/S-type (class I) glutaredoxins (Grxs) act as oxidoreductases, while CGFS-type (class II) Grxs act as FeS cluster transferases. Here we show that the key determinant of Grx function is a distinct loop structure adjacent to the active site. Engineering of a CxxC/S-type Grx with a CGFS-type loop switched its function from oxidoreductase to FeS transferase. Engineering of a CGFS-type Grx with a CxxC/S-type loop abolished FeS transferase activity and activated the oxidative half reaction of the oxidoreductase. The reductive half-reaction, requiring the interaction with a second GSH molecule, was enabled by switching additional residues in the active site. We explain how subtle structural differences, mostly depending on the structure of one particular loop, act in concert to determine Grx function.

Date: 2020
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DOI: 10.1038/s41467-020-17323-0

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