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| | <StructureSection load='1al8' size='340' side='right'caption='[[1al8]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1al8' size='340' side='right'caption='[[1al8]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1al8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spiol Spiol]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AL8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1al8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AL8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DHP:3-DECYL-2,5-DIOXO-4-HYDROXY-3-PYRROLINE'>DHP</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 2.2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(S)-2-hydroxy-acid_oxidase (S)-2-hydroxy-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.15 1.1.3.15] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHP:3-DECYL-2,5-DIOXO-4-HYDROXY-3-PYRROLINE'>DHP</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></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=1al8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al8 OCA], [http://pdbe.org/1al8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1al8 RCSB], [http://www.ebi.ac.uk/pdbsum/1al8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1al8 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=1al8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al8 OCA], [https://pdbe.org/1al8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1al8 RCSB], [https://www.ebi.ac.uk/pdbsum/1al8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1al8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GOX_SPIOL GOX_SPIOL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Spiol]] | + | [[Category: Spinacia oleracea]] |
| - | [[Category: Lindqvist, Y]] | + | [[Category: Lindqvist Y]] |
| - | [[Category: Stenberg, K]] | + | [[Category: Stenberg K]] |
| - | [[Category: Drug design]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Inhibitor binding]]
| + | |
| Structural highlights
Function
GOX_SPIOL
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
A key step in plant photorespiration, the oxidation of glycolate to glyoxylate, is carried out by the peroxisomal flavoprotein glycolate oxidase (EC 1.1.3.15). The three-dimensional structure of this alpha/beta barrel protein has been refined to 2 A resolution (Lindqvist Y. 1989. J Mol Biol 209:151-166). FMN dependent glycolate oxidase is a member of the family of alpha-hydroxy acid oxidases. Here we describe the crystallization and structure determination of two inhibitor complexes of the enzyme, TKP (3-Decyl-2,5-dioxo-4-hydroxy-3-pyrroline) and TACA (4-Carboxy-5-(1-pentyl)hexylsulfanyl-1,2,3-triazole). The structure of the TACA complex has been refined to 2.6 A resolution and the TKP complex, solved with molecular replacement, to 2.2 A resolution. The Rfree for the TACA and TKP complexes are 24.2 and 25.1%, respectively. The overall structures are very similar to the unliganded holoenzyme, but a closer examination of the active site reveals differences in the positioning of the flavin isoalloxazine ring and a displaced flexible loop in the TKP complex. The two inhibitors differ in binding mode and hydrophobic interactions, and these differences are reflected by the very different Ki values for the inhibitors, 16 nM for TACA and 4.8 microM for TKP. Implications of the structures of these enzyme-inhibitor complexes for the model for substrate binding and catalysis proposed from the holo-enzyme structure are discussed.
Three-dimensional structures of glycolate oxidase with bound active-site inhibitors.,Stenberg K, Lindqvist Y Protein Sci. 1997 May;6(5):1009-15. PMID:9144771[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stenberg K, Lindqvist Y. Three-dimensional structures of glycolate oxidase with bound active-site inhibitors. Protein Sci. 1997 May;6(5):1009-15. PMID:9144771
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