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| | <StructureSection load='5zbn' size='340' side='right'caption='[[5zbn]], [[Resolution|resolution]] 2.32Å' scene=''> | | <StructureSection load='5zbn' size='340' side='right'caption='[[5zbn]], [[Resolution|resolution]] 2.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zbn]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Nicbe Nicbe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZBN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZBN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zbn]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_benthamiana Nicotiana benthamiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZBN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.32Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zbm|5zbm]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GOX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4100 NICBE])</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=5zbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zbn OCA], [https://pdbe.org/5zbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zbn RCSB], [https://www.ebi.ac.uk/pdbsum/5zbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zbn ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zbn OCA], [http://pdbe.org/5zbn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zbn RCSB], [http://www.ebi.ac.uk/pdbsum/5zbn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zbn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E1AXT8_NICBE E1AXT8_NICBE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nicbe]] | + | [[Category: Nicotiana benthamiana]] |
| - | [[Category: Chen, Z]] | + | [[Category: Chen Z]] |
| - | [[Category: Liu, Y]] | + | [[Category: Liu Y]] |
| - | [[Category: Enzyme kinetic]]
| + | |
| - | [[Category: Oligomerization]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Sax]]
| + | |
| Structural highlights
Function
E1AXT8_NICBE
Publication Abstract from PubMed
Glycolate oxidase (GOX), a flavin mononucleotide (FMN)-dependent enzyme, modulates reactive oxygen species-mediated signal transduction in green plants. It has been a target protein for crop improvement because of performing a key step in photorespiration that causes the energy losses. In human, GOX is involved in the production of oxalate, which is a key metabolite in the formation of kidney stone. Here, we report the first apo-GOX structure and its complex structure with cofactor FMN from Nicotiana benthamiana by X-ray crystallography. The binding of FMN induces a pronounced conformational change of GOX tetramer. Interestingly, a conserved pH sensor found among different species might directly regulate the binding of FMN and the enzyme activity. Combined with enzymatic experiments and biophysical analyses, we provide new insights in the molecular mechanism of regulating GOX biological activity reversibly and new methods of agricultural production and clinical application.
Structures of glycolate oxidase from Nicotiana benthamiana reveal a conserved pH sensor affecting the binding of FMN.,Liu Y, Wu W, Chen Z Biochem Biophys Res Commun. 2018 Sep 18;503(4):3050-3056. doi:, 10.1016/j.bbrc.2018.08.092. Epub 2018 Aug 22. PMID:30143257[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu Y, Wu W, Chen Z. Structures of glycolate oxidase from Nicotiana benthamiana reveal a conserved pH sensor affecting the binding of FMN. Biochem Biophys Res Commun. 2018 Sep 18;503(4):3050-3056. doi:, 10.1016/j.bbrc.2018.08.092. Epub 2018 Aug 22. PMID:30143257 doi:http://dx.doi.org/10.1016/j.bbrc.2018.08.092
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