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| | <StructureSection load='2whd' size='340' side='right'caption='[[2whd]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='2whd' size='340' side='right'caption='[[2whd]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2whd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Barley Barley]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WHD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2whd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WHD FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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]] 2.6Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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=2whd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2whd OCA], [https://pdbe.org/2whd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2whd RCSB], [https://www.ebi.ac.uk/pdbsum/2whd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2whd 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=2whd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2whd OCA], [https://pdbe.org/2whd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2whd RCSB], [https://www.ebi.ac.uk/pdbsum/2whd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2whd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A9LN30_HORVV A9LN30_HORVV] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Barley]] | + | [[Category: Hordeum vulgare]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thioredoxin-disulfide reductase]]
| + | [[Category: Finnie C]] |
| - | [[Category: Finnie, C]] | + | [[Category: Hagglund P]] |
| - | [[Category: Hagglund, P]] | + | [[Category: Henriksen A]] |
| - | [[Category: Henriksen, A]] | + | [[Category: Kirkensgaard KG]] |
| - | [[Category: Kirkensgaard, K G]] | + | [[Category: Svensson B]] |
| - | [[Category: Svensson, B]] | + | |
| - | [[Category: Disulfide oxidoreductase]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Germination]]
| + | |
| - | [[Category: Ntr]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Redox regulation]]
| + | |
| - | [[Category: Redox-active center]]
| + | |
| - | [[Category: Seed development]]
| + | |
| Structural highlights
Function
A9LN30_HORVV
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Thioredoxins (Trxs) are protein disulfide reductases that regulate the intracellular redox environment and are important for seed germination in plants. Trxs are in turn regulated by NADPH-dependent thioredoxin reductases (NTRs), which provide reducing equivalents to Trx using NADPH to recycle Trxs to the active form. Here, the first crystal structure of a cereal NTR, HvNTR2 from Hordeum vulgare (barley), is presented, which is also the first structure of a monocot plant NTR. The structure was determined at 2.6 A resolution and refined to an R(cryst) of 19.0% and an R(free) of 23.8%. The dimeric protein is structurally similar to the structures of AtNTR-B from Arabidopsis thaliana and other known low-molecular-weight NTRs. However, the relative position of the two NTR cofactor-binding domains, the FAD and the NADPH domains, is not the same. The NADPH domain is rotated by 25 degrees and bent by a 38% closure relative to the FAD domain in comparison with AtNTR-B. The structure may represent an intermediate between the two conformations described previously: the flavin-oxidizing (FO) and the flavin-reducing (FR) conformations. Here, analysis of interdomain contacts as well as phylogenetic studies lead to the proposal of a new reaction scheme in which NTR-Trx interactions mediate the FO to FR transformation.
Structure of Hordeum vulgare NADPH-dependent thioredoxin reductase 2. Unwinding the reaction mechanism.,Kirkensgaard KG, Hagglund P, Finnie C, Svensson B, Henriksen A Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):932-41. Epub 2009, Aug 14. PMID:19690371[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kirkensgaard KG, Hagglund P, Finnie C, Svensson B, Henriksen A. Structure of Hordeum vulgare NADPH-dependent thioredoxin reductase 2. Unwinding the reaction mechanism. Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):932-41. Epub 2009, Aug 14. PMID:19690371 doi:10.1107/S0907444909021817
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