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| | ==Solution Structure of Thioredoxin h1 from Arabidopsis Thaliana== | | ==Solution Structure of Thioredoxin h1 from Arabidopsis Thaliana== |
| - | <StructureSection load='1xfl' size='340' side='right'caption='[[1xfl]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1xfl' size='340' side='right'caption='[[1xfl]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xfl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XFL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xfl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XFL FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At3g51030 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1xfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfl OCA], [https://pdbe.org/1xfl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xfl RCSB], [https://www.ebi.ac.uk/pdbsum/1xfl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfl ProSAT], [https://www.topsan.org/Proteins/CESG/1xfl TOPSAN]</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=1xfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfl OCA], [https://pdbe.org/1xfl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xfl RCSB], [https://www.ebi.ac.uk/pdbsum/1xfl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfl ProSAT], [https://www.topsan.org/Proteins/CESG/1xfl TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TRXH1_ARATH TRXH1_ARATH]] Thiol-disulfide oxidoreductase involved in the redox regulation of a number of cytosolic enzymes. Activates the cytosolic malate dehydrogenase (MDH) probably by reducing an interchain disulfid bond of the inactive MDH homodimer. Possesses insulin disulfide bonds reducing activity.<ref>PMID:16945919</ref>
| + | [https://www.uniprot.org/uniprot/TRXH1_ARATH TRXH1_ARATH] Thiol-disulfide oxidoreductase involved in the redox regulation of a number of cytosolic enzymes. Activates the cytosolic malate dehydrogenase (MDH) probably by reducing an interchain disulfid bond of the inactive MDH homodimer. Possesses insulin disulfide bonds reducing activity.<ref>PMID:16945919</ref> |
| | == 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: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Lytle BL]] |
| - | [[Category: Lytle, B L]] | + | [[Category: Markley JL]] |
| - | [[Category: Markley, J L]] | + | [[Category: Peterson FC]] |
| - | [[Category: Peterson, F C]] | + | [[Category: Sampath S]] |
| - | [[Category: Sampath, S]] | + | [[Category: Shahan M]] |
| - | [[Category: Shahan, M]] | + | [[Category: Tyler E]] |
| - | [[Category: Tyler, E]] | + | [[Category: Vinarov D]] |
| - | [[Category: Vinarov, D]] | + | [[Category: Volkman BF]] |
| - | [[Category: Volkman, B F]] | + | |
| - | [[Category: At3g51030]]
| + | |
| - | [[Category: Cesg]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Thioredoxin]]
| + | |
| Structural highlights
Function
TRXH1_ARATH Thiol-disulfide oxidoreductase involved in the redox regulation of a number of cytosolic enzymes. Activates the cytosolic malate dehydrogenase (MDH) probably by reducing an interchain disulfid bond of the inactive MDH homodimer. Possesses insulin disulfide bonds reducing activity.[1]
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
Present in virtually every species, thioredoxins catalyze disulfide/dithiol exchange with various substrate proteins. While the human genome contains a single thioredoxin gene, plant thioredoxins are a complex protein family. A total of 19 different thioredoxin genes in six subfamilies has emerged from analysis of the Arabidopsis thaliana genome. Some function specifically in mitochondrial and chloroplast redox signaling processes, but target substrates for a group of eight thioredoxin proteins comprising the h subfamily are largely uncharacterized. In the course of a structural genomics effort directed at the recently completed A. thaliana genome, we determined the structure of thioredoxin h1 (At3g51030.1) in the oxidized state. The structure, defined by 1637 NMR-derived distance and torsion angle constraints, displays the conserved thioredoxin fold, consisting of a five-stranded beta-sheet flanked by four helices. Redox-dependent chemical shift perturbations mapped primarily to the conserved WCGPC active-site sequence and other nearby residues, but distant regions of the C-terminal helix were also affected by reduction of the active-site disulfide. Comparisons of the oxidized A. thaliana thioredoxin h1 structure with an h-type thioredoxin from poplar in the reduced state revealed structural differences in the C-terminal helix but no major changes in the active site conformation.
Solution structure of thioredoxin h1 from Arabidopsis thaliana.,Peterson FC, Lytle BL, Sampath S, Vinarov D, Tyler E, Shahan M, Markley JL, Volkman BF Protein Sci. 2005 Aug;14(8):2195-200. Epub 2005 Jun 29. PMID:15987893[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hara S, Motohashi K, Arisaka F, Romano PG, Hosoya-Matsuda N, Kikuchi N, Fusada N, Hisabori T. Thioredoxin-h1 reduces and reactivates the oxidized cytosolic malate dehydrogenase dimer in higher plants. J Biol Chem. 2006 Oct 27;281(43):32065-71. Epub 2006 Aug 31. PMID:16945919 doi:http://dx.doi.org/10.1074/jbc.M605784200
- ↑ Peterson FC, Lytle BL, Sampath S, Vinarov D, Tyler E, Shahan M, Markley JL, Volkman BF. Solution structure of thioredoxin h1 from Arabidopsis thaliana. Protein Sci. 2005 Aug;14(8):2195-200. Epub 2005 Jun 29. PMID:15987893 doi:10.1110/ps.051477905
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