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| | <StructureSection load='7c65' size='340' side='right'caption='[[7c65]], [[Resolution|resolution]] 1.10Å' scene=''> | | <StructureSection load='7c65' size='340' side='right'caption='[[7c65]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7c65]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C65 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7C65 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7c65]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C65 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At1g03680, F21B7.28, F21B7_7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7c65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c65 OCA], [http://pdbe.org/7c65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7c65 RCSB], [http://www.ebi.ac.uk/pdbsum/7c65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7c65 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7c65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c65 OCA], [https://pdbe.org/7c65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c65 RCSB], [https://www.ebi.ac.uk/pdbsum/7c65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c65 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRXM1_ARATH 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.<ref>PMID:19631646</ref> <ref>PMID:19825612</ref> | + | [https://www.uniprot.org/uniprot/TRXM1_ARATH 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.<ref>PMID:19631646</ref> <ref>PMID:19825612</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Juniar, L]] | + | [[Category: Juniar L]] |
| - | [[Category: Kurisu, G]] | + | [[Category: Kurisu G]] |
| - | [[Category: Tanaka, H]] | + | [[Category: Tanaka H]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Trx m1]]
| + | |
| Structural highlights
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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nee G, Zaffagnini M, Trost P, Issakidis-Bourguet E. Redox regulation of chloroplastic glucose-6-phosphate dehydrogenase: a new role for f-type thioredoxin. FEBS Lett. 2009 Sep 3;583(17):2827-32. doi: 10.1016/j.febslet.2009.07.035. Epub, 2009 Jul 23. PMID:19631646 doi:http://dx.doi.org/10.1016/j.febslet.2009.07.035
- ↑ Marri L, Zaffagnini M, Collin V, Issakidis-Bourguet E, Lemaire SD, Pupillo P, Sparla F, Miginiac-Maslow M, Trost P. Prompt and easy activation by specific thioredoxins of calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex. Mol Plant. 2009 Mar;2(2):259-69. doi: 10.1093/mp/ssn061. Epub 2008 Oct 3. PMID:19825612 doi:http://dx.doi.org/10.1093/mp/ssn061
- ↑ Juniar L, Tanaka H, Yoshida K, Hisabori T, Kurisu G. Structural basis for Thioredoxin isoform-based fine tuning of Ferredoxin-Thioredoxin Reductase activity. Protein Sci. 2020 Oct 4. doi: 10.1002/pro.3964. PMID:33015914 doi:http://dx.doi.org/10.1002/pro.3964
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