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| | <StructureSection load='5yry' size='340' side='right'caption='[[5yry]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='5yry' size='340' side='right'caption='[[5yry]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yry]] 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=5YRY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YRY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yry]] 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=5YRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YRY FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APR1, PRH19, At4g04610, F4H6.13 ([http://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">X-ray diffraction, [[Resolution|Resolution]] 2.698Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylyl-sulfate_reductase_(glutathione) Adenylyl-sulfate reductase (glutathione)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.9 1.8.4.9] </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=5yry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yry OCA], [https://pdbe.org/5yry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yry RCSB], [https://www.ebi.ac.uk/pdbsum/5yry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yry ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5yry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yry OCA], [http://pdbe.org/5yry PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yry RCSB], [http://www.ebi.ac.uk/pdbsum/5yry PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yry ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/APR1_ARATH APR1_ARATH]] Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons. | + | [https://www.uniprot.org/uniprot/APR1_ARATH APR1_ARATH] Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Sulfur is an essential nutrient that can be converted into utilizable metabolic forms to produce sulfur-containing metabolites in plant. Adenosine 5'-phosphosulfate (APS) reductase (APR) plays a vital role in catalyzing the reduction of activated sulfate to sulfite, which requires glutathione. Previous studies have shown that the C-terminal domain of APR acts as a glutathione-dependent reductase. The crystal structure of the C-terminal redox domain of Arabidopsis APR1 (AtAPR1) shows a conserved alpha/beta thioredoxin fold, but not a glutaredoxin fold. Further biochemical studies of the redox domain from AtAPR1 provided evidence to support the structural observation. Collectively, our results provide structural and biochemical information to explain how the thioredoxin fold exerts the glutaredoxin function in APR.
| + | |
| - | | + | |
| - | C-terminal Redox Domain of Arabidopsis APR1 is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function.,Chen FF, Chien CY, Cho CC, Chang YY, Hsu CH Antioxidants (Basel). 2019 Oct 8;8(10). pii: antiox8100461. doi:, 10.3390/antiox8100461. PMID:31597378<ref>PMID:31597378</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5yry" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hsu, C H]] | + | [[Category: Hsu CH]] |
| - | [[Category: Aps reductase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Redox domain]]
| + | |
| - | [[Category: Sulfer assimilatory]]
| + | |
