7c65 | pdb_00007c65

Crystal structure of thioredoxin m1

spinqualitylabelsall models 7c65, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7c65 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.1Å Ligands: NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRXM1_ARATH Thiol-disulfide oxidoreductase involved in the redox regulation of enzymes of both reductive pentose phosphate pathway (Calvin-Benson cycle) and oxidative pentose phosphate pathway. Under reducing conditions, activates the glyceraldehyde-3-phosphate dehydrogenase and the phosphoribulokinase, and inhibits. the glucose-6-phosphate dehydrogenase. Activates NADP-malate dehydrogenase. Publication Abstract from PubMed 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 ten Trx isoforms in Arabidopsis thaliana can 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-m structures. 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. This article is protected by copyright. All rights reserved. Structural basis for Thioredoxin isoform-based fine tuning of Ferredoxin-Thioredoxin Reductase activity.,Juniar L, Tanaka H, Yoshida K, Hisabori T, Kurisu G Protein Sci. 2020 Oct 4. doi: 10.1002/pro.3964. PMID:33015914 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioredoxin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA