6I1C

Crystal structure of Chlamydomonas reinhardtii thioredoxin f2

Summary for 6I1C

• Entry DOI: 10.2210/pdb6i1c/pdb
• Descriptor: thioredoxin f2 (2 entities in total)
• Functional Keywords: f-type cytosolic thioredoxin oxidized, electron transport
• Biological source: Chlamydomonas reinhardtii (Chlamydomonas smithii)
• Total number of polymer chains: 3
• Total formula weight: 43309.99

Authors

Lemaire, S.D.,Tedesco, D.,Crozet, P.,Michelet, L.,Fermani, S.,Zaffagnini, M.,Henri, J. (deposition date: 2018-10-28, release date: 2018-12-05, Last modification date: 2024-05-01)

Primary citation

Lemaire, S.D.,Tedesco, D.,Crozet, P.,Michelet, L.,Fermani, S.,Zaffagnini, M.,Henri, J.
Crystal Structure of Chloroplastic Thioredoxin f2 fromChlamydomonas reinhardtiiReveals Distinct Surface Properties.
Antioxidants (Basel), 7:-, 2018

PubMed Abstract: 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.

PubMed: 30477165
DOI: 10.3390/antiox7120171

Experimental method

X-RAY DIFFRACTION (2.01 Å)