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Open AccessArticle

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

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Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, Unité Mixte de Recherche 8226 CNRS Sorbonne Université, 13 rue Pierre et Marie Curie, 75005 Paris, France
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Bio-Pharmaceutical Analysis Section (Bio-PhASe), Department of Pharmacy and Biotechnology, University of Bologna, via Belmeloro 6, 40126 Bologna, Italy
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Department of Chemistry “Giacomo Ciamician”, University of Bologna, via Selmi 2, 40126 Bologna, Italy
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Laboratory of Molecular Plant Physiology, Department of Pharmacy and Biotechnology, University of Bologna, via Irnerio 42, 40126 Bologna, Italy
*
Authors to whom correspondence should be addressed.
Antioxidants 2018, 7(12), 171; https://doi.org/10.3390/antiox7120171
Received: 31 October 2018 / Revised: 13 November 2018 / Accepted: 20 November 2018 / Published: 23 November 2018
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems)
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 Chlamydomonas reinhardtii, 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 C. reinhardtii. 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. View Full-Text
Keywords: thioredoxin; Calvin-Benson cycle; photosynthesis; carbon fixation; chloroplast; macromolecular crystallography; protein-protein recognition; electrostatic surface; Chlamydomonas reinhardtii thioredoxin; Calvin-Benson cycle; photosynthesis; carbon fixation; chloroplast; macromolecular crystallography; protein-protein recognition; electrostatic surface; Chlamydomonas reinhardtii
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Lemaire, S.D.; Tedesco, D.; Crozet, P.; Michelet, L.; Fermani, S.; Zaffagnini, M.; Henri, J. Crystal Structure of Chloroplastic Thioredoxin f2 from Chlamydomonas reinhardtii Reveals Distinct Surface Properties. Antioxidants 2018, 7, 171.

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