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

被引:16
|
作者
Lemaire, Stephane D. [1 ]
Tedesco, Daniele [2 ]
Crozet, Pierre [1 ]
Michelet, Laure [1 ]
Fermani, Simona [3 ]
Zaffagnini, Mirko [4 ]
Henri, Julien [1 ]
机构
[1] Sorbonne Univ, CNRS, Unite Mixte Rech 8226, Inst Biol Phys Chim,Lab Biol Mol & Cellularies Eu, 13 Rue Pierre & Marie Curie, F-75005 Paris, France
[2] Univ Bologna, Dept Pharm & Biotechnol, Biopharmaceut Anal Sect Bio PhASe, Via Belmeloro 6, I-40126 Bologna, Italy
[3] Univ Bologna, Dept Chem Giacomo Ciamician, Via Selmi 2, I-40126 Bologna, Italy
[4] Univ Bologna, Dept Pharm & Biotechnol, Lab Mol Plant Physiol, Via Irnerio 42, I-40126 Bologna, Italy
关键词
thioredoxin; Calvin-Benson cycle; photosynthesis; carbon fixation; chloroplast; macromolecular crystallography; protein-protein recognition; electrostatic surface; Chlamydomonas reinhardtii; PHOTOSYNTHETIC GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; OXIDATION-REDUCTION PROPERTIES; ESCHERICHIA-COLI THIOREDOXIN; MOLECULAR-MECHANISMS; REDOX REGULATION; PLASTIDIAL THIOREDOXINS; SECONDARY STRUCTURE; GREEN-ALGA; PROTEIN; RECOGNITION;
D O I
10.3390/antiox7120171
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
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页数:17
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