Crystal Structure of Chloroplastic Thioredoxin f2 from Chlamydomonas reinhardtii Reveals Distinct Surface Properties

Protein disulfide reduction by thioredoxins (TRXs) controls the conformation of enzyme active sites and their multimeric complex formation. TRXs are small oxidoreductases that are broadly conserved in all living organisms. In photosynthetic eukaryotes, TRXs form a large multigenic family, and they h...

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Bibliographic Details
Published in:Antioxidants 2018-11, Vol.7 (12), p.171
Main Authors: Lemaire, Stéphane D, Tedesco, Daniele, Crozet, Pierre, Michelet, Laure, Fermani, Simona, Zaffagnini, Mirko, Henri, Julien
Format: Article
Language:English
Subjects:
Biochemistry, Molecular Biology
Calvin-Benson cycle
Carbon fixation
Cellular Biology
Chlamydomonas reinhardtii
chloroplast
Chloroplasts
Crystal structure
Cytosol
Datasets
Dehydrogenases
electrostatic surface
Enzymes
Eukaryotes
Isoenzymes
Kinases
Life Sciences
macromolecular crystallography
Mitochondria
Peptides
photosynthesis
Polyethylene glycol
protein-protein recognition
Proteins
Surface properties
Thioredoxin
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Summary:Protein disulfide reduction by thioredoxins (TRXs) controls the conformation of enzyme active sites and their multimeric complex formation. TRXs are small oxidoreductases that are broadly conserved in all living organisms. In photosynthetic eukaryotes, TRXs form a large multigenic family, and they have been classified in different types: f, m, x, y, and z types are chloroplastic, while o and h types are located in mitochondria and cytosol. In the model unicellular alga , the TRX family contains seven types, with f- and h-types represented by two isozymes. Type-f TRXs interact specifically with targets in the chloroplast, controlling photosynthetic carbon fixation by the Calvin⁻Benson cycle. We solved the crystal structures of TRX f2 and TRX h1 from . The systematic comparison of their atomic features revealed a specific conserved electropositive crown around the active site of TRX f, complementary to the electronegative surface of their targets. We postulate that this surface provides specificity to each type of TRX.
ISSN:2076-3921
2076-3921
DOI:10.3390/antiox7120171