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

  • Despite their very close structural similarity, CxxC/S-type (class I) glutaredoxins (Grxs) actas oxidoreductases, while CGFS-type (class II) Grxs act as FeS cluster transferases. Here weshow that the key determinant of Grx function is a distinct loop structure adjacent to theactive site. Engineering of a CxxC/S-type Grx with a CGFS-type loop switched its functionfrom oxidoreductase to FeS transferase. Engineering of a CGFS-type Grx with a CxxC/S-typeloop abolished FeS transferase activity and activated the oxidative half reaction of the oxi-doreductase. The reductive half-reaction, requiring the interaction with a second GSHmolecule, was enabled by switching additional residues in the active site. We explain howsubtle structural differences, mostly depending on the structure of one particular loop, act inconcert to determine Grx function.

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Author: Manuela GellertORCiD, Daniel Trnka, Anna D. Engelke, Anna Moseler, Faruq Hossain, Tobias Lindenberg, Luca Pedroletti, Benjamin Odermatt, Joao Souza, Agnieszka Bronowska, Tobias Dick, Uli Mühlenhoff, Andreas Meyer, Carsten Berndt, Christopher Horst Lillig
Parent Title (English):Nature
Publisher:Springer Nature
Place of publication:London
Document Type:Article
Date of first Publication:2020/06/18
Release Date:2021/03/23
Faculties:Universitätsmedizin / Institut für Med. Biochemie u. Molekularbiologie
Licence (German):License LogoCreative Commons - Namensnennung