期刊
PROTEIN SCIENCE
卷 29, 期 12, 页码 2538-2545出版社
WILEY
DOI: 10.1002/pro.3964
关键词
electron transport; ferredoxin-reductase; thioredoxin; thioredoxin; x-ray crystal structure
资金
- Japan Society for the Promotion of Science [16H06556, 16H06560, 19H03241]
- Ministry of Education, Culture, Sports, Science and Technology
- Grants-in-Aid for Scientific Research [16H06560, 19H03241] Funding Source: KAKEN
Photosynthetic electron transport occurs on the thylakoid membrane of chloroplasts. Ferredoxin (Fd), the final acceptor in the electron transport chain, distributes electrons to several Fd-dependent enzymes including Fd-thioredoxin reductase (FTR). A cascade from Fd to FTR further reduces Thioredoxin (Trx), which tunes the activity of target metabolic enzymes eventually in a light-dependent manner. We previously reported that 10 Trx isoforms inArabidopsis thalianacan be clustered into three classes based on the kinetics of the FTR-dependent reduction (high-, middle-, and low-efficiency classes). In this study, we determined the X-ray structure of three electron transfer complexes of FTR and Trx isoform, Trx-y1, Trx-f2, and Trx-m2, as representative examples of each class. Superposition of the FTR structure with/without Trx showed no main chain structural changes upon complex formation. There was no significant conformational change for single and complexed Trx-mstructures. Nonetheless, the interface of FTR:Trx complexes displayed significant variation. Comparative analysis of the three structures showed two types of intermolecular interactions; (i) common interactions shared by all three complexes and (ii) isoform-specific interactions, which might be important for fine-tuning FTR:Trx activity. Differential electrostatic potentials of Trx isoforms may be key to isoform-specific interactions.
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