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Crystal structure of chloroplastic thioredoxin z defines a type-specific target recognition

TitleCrystal structure of chloroplastic thioredoxin z defines a type-specific target recognition
Publication TypeJournal Article
Year of Publication2021
AuthorsLe Moigne, T, Gurrieri, L, Crozet, P, Marchand, CH, Zaffagnini, M, Sparla, F, Lemaire, SD, Henri, J
JournalThe Plant Journal
Volume107
Pagination434-447
KeywordsCalvin–Benson cycle, Photosynthesis, protein structure, protein–protein interactions, redox post-translational modifications, Thioredoxins
Abstract

Summary Thioredoxins (TRXs) are ubiquitous disulfide oxidoreductases structured according to a highly conserved fold. TRXs are involved in a myriad of different processes through a common chemical mechanism. Plant TRXs evolved into seven types with diverse subcellular localization and distinct protein target selectivity. Five TRX types coexist in the chloroplast, with yet scarcely described specificities. We solved the crystal structure of a chloroplastic z-type TRX, revealing a conserved TRX fold with an original electrostatic surface potential surrounding the redox site. This recognition surface is distinct from all other known TRX types from plant and non-plant sources and is exclusively conserved in plant z-type TRXs. We show that this electronegative surface endows thioredoxin z (TRXz) with a capacity to activate the photosynthetic Calvin–Benson cycle enzyme phosphoribulokinase. The distinct electronegative surface of TRXz thereby extends the repertoire of TRX–target recognitions.

URLhttps://onlinelibrary.wiley.com/doi/abs/10.1111/tpj.15300
DOI10.1111/tpj.15300

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