7p9d: Difference between revisions
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==Crystal structure of Chlamydomonas reinhardtii NADPH Dependent Thioredoxin Reductase 1 domain== | ==Crystal structure of Chlamydomonas reinhardtii NADPH Dependent Thioredoxin Reductase 1 domain== | ||
<StructureSection load='7p9d' size='340' side='right'caption='[[7p9d]]' scene=''> | <StructureSection load='7p9d' size='340' side='right'caption='[[7p9d]], [[Resolution|resolution]] 1.99Å' 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=7P9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P9D FirstGlance]. <br> | <table><tr><td colspan='2'>[[7p9d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P9D FirstGlance]. <br> | ||
</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=7p9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p9d OCA], [https://pdbe.org/7p9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p9d RCSB], [https://www.ebi.ac.uk/pdbsum/7p9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p9d ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=7p9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p9d OCA], [https://pdbe.org/7p9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p9d RCSB], [https://www.ebi.ac.uk/pdbsum/7p9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p9d ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In plant chloroplasts, thiol regulation is driven by two systems. One relies on the activity of thioredoxins through their light dependent reduction by ferredoxin via a ferredoxin-thioredoxin reductase (FTR). In the other system, a NADPH-dependent redox regulation is driven by a NADPH-thioredoxin reductase C (NTRC). While the thioredoxin system has been deeply studied, a more thorough understanding of the function of this plant specific NTRC is desirable. NTRC is a single polypeptide harbouring a thioredoxin domain (Trx) at the C-terminus of a NADPH-dependent Thioredoxin reductase (TrxR). To provide functional and structural insights, we studied the crystal structure of the TrxR domain of the NTRC from Chlamydomonas reinhardtii (CrNTRC, Cre01.g054150.t1.2) and its Cys136Ser (C136S) mutant, which is characterized by the mutation of the resolving cysteine in the active site of the TrxR domain. Furthermore, we confirmed the role of NTRC as electron donor for 2-Cys peroxiredoxin (PRX) also in C. reinhardtii. The structural data of TrxR were employed to develop a scheme of action which addresses electron transfer between TrxR and Trx of NTRC and between NTRC and its substrates. | |||
Structural analysis revealed a novel conformation of the NTRC reductase domain from Chlamydomonas reinhardtii.,Marchetti GM, Fusser F, Singh RK, Brummel M, Koch O, Kummel D, Hippler M J Struct Biol. 2021 Dec 30;214(1):107829. doi: 10.1016/j.jsb.2021.107829. PMID:34974142<ref>PMID:34974142</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7p9d" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hippler M]] | [[Category: Thioredoxin-disulfide reductase]] | ||
[[Category: Kuemmel D]] | [[Category: Hippler, M]] | ||
[[Category: Marchetti | [[Category: Kuemmel, D]] | ||
[[Category: Singh | [[Category: Marchetti, G M]] | ||
[[Category: Singh, R K]] | |||
[[Category: Fad binding domain]] | |||
[[Category: Flavoprotein]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 10:41, 19 January 2022
Crystal structure of Chlamydomonas reinhardtii NADPH Dependent Thioredoxin Reductase 1 domainCrystal structure of Chlamydomonas reinhardtii NADPH Dependent Thioredoxin Reductase 1 domain
Structural highlights
Publication Abstract from PubMedIn plant chloroplasts, thiol regulation is driven by two systems. One relies on the activity of thioredoxins through their light dependent reduction by ferredoxin via a ferredoxin-thioredoxin reductase (FTR). In the other system, a NADPH-dependent redox regulation is driven by a NADPH-thioredoxin reductase C (NTRC). While the thioredoxin system has been deeply studied, a more thorough understanding of the function of this plant specific NTRC is desirable. NTRC is a single polypeptide harbouring a thioredoxin domain (Trx) at the C-terminus of a NADPH-dependent Thioredoxin reductase (TrxR). To provide functional and structural insights, we studied the crystal structure of the TrxR domain of the NTRC from Chlamydomonas reinhardtii (CrNTRC, Cre01.g054150.t1.2) and its Cys136Ser (C136S) mutant, which is characterized by the mutation of the resolving cysteine in the active site of the TrxR domain. Furthermore, we confirmed the role of NTRC as electron donor for 2-Cys peroxiredoxin (PRX) also in C. reinhardtii. The structural data of TrxR were employed to develop a scheme of action which addresses electron transfer between TrxR and Trx of NTRC and between NTRC and its substrates. Structural analysis revealed a novel conformation of the NTRC reductase domain from Chlamydomonas reinhardtii.,Marchetti GM, Fusser F, Singh RK, Brummel M, Koch O, Kummel D, Hippler M J Struct Biol. 2021 Dec 30;214(1):107829. doi: 10.1016/j.jsb.2021.107829. PMID:34974142[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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