Crystal Structure of Chloroplastic Thioredoxin f2 from <i>Chlamydomonas reinhardtii</i> Reveals Distinct Surface Properties

Crystal Structure of Chloroplastic Thioredoxin f2 from <i>Chlamydomonas reinhardtii</i> Reveals Distinct Surface Properties

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 h...

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Bibliographic Details
Main Authors: Stéphane D. Lemaire, Daniele Tedesco, Pierre Crozet, Laure Michelet, Simona Fermani, Mirko Zaffagnini, Julien Henri
Format: Article
Language:English
Published: MDPI AG 2018-11-01
Series:Antioxidants
Subjects:
thioredoxin
Calvin-Benson cycle
photosynthesis
carbon fixation
chloroplast
macromolecular crystallography
protein-protein recognition
electrostatic surface
<i>Chlamydomonas reinhardtii</i>
Online Access:https://www.mdpi.com/2076-3921/7/12/171

Internet

https://www.mdpi.com/2076-3921/7/12/171

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