期刊
PLANT JOURNAL
卷 107, 期 2, 页码 434-447出版社
WILEY
DOI: 10.1111/tpj.15300
关键词
Calvin– Benson cycle; Photosynthesis; protein structure; protein– protein interactions; redox post‐ translational modifications; thioredoxins
资金
- CNRS
- Sorbonne Universite
- Agence Nationale de la Recherche grant LABEX DYNAMO [11-LABX-0011]
- Agence Nationale de la Recherche grant CALVINDESIGN [ANR-17-CE05-001]
- Agence Nationale de la Recherche grant CALVINTERACT [ANR-19-CE11-0009]
- Italian Ministry of University and Research [PON ARS01 00881]
- Agence Nationale de la Recherche (ANR) [ANR-19-CE11-0009] Funding Source: Agence Nationale de la Recherche (ANR)
Thioredoxins (TRXs) are a class of disulfide oxidoreductases with a highly conserved fold, plant TRXs evolved into seven types, with z-type TRX having a distinct electronegative surface that can activate the photosynthetic enzyme phosphoribulokinase.
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.
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