7c3f: Difference between revisions
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==== | ==Crystal structure of ferredoxin: thioredoxin reductase and thioredoxin m2 complex== | ||
<StructureSection load='7c3f' size='340' side='right'caption='[[7c3f]]' scene=''> | <StructureSection load='7c3f' size='340' side='right'caption='[[7c3f]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[7c3f]] is a 23 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=7C3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C3F FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3986Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=7c3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c3f OCA], [https://pdbe.org/7c3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c3f RCSB], [https://www.ebi.ac.uk/pdbsum/7c3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c3f ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/FTRC_ARATH FTRC_ARATH] Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.[UniProtKB:Q55389] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:33015914</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7c3f" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ferredoxin thioredoxin reductase|Ferredoxin thioredoxin reductase]] | |||
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Juniar L]] | ||
[[Category: Kurisu G]] | |||
[[Category: Tanaka H]] | |||
Latest revision as of 16:28, 6 November 2024
Crystal structure of ferredoxin: thioredoxin reductase and thioredoxin m2 complexCrystal structure of ferredoxin: thioredoxin reductase and thioredoxin m2 complex
Structural highlights
FunctionFTRC_ARATH Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.[UniProtKB:Q55389] Publication Abstract from PubMedPhotosynthetic 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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