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| | <StructureSection load='1v03' size='340' side='right'caption='[[1v03]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1v03' size='340' side='right'caption='[[1v03]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1v03]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Andropogon_sorghum Andropogon sorghum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V03 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v03]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sorghum_bicolor Sorghum bicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V03 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1v02|1v02]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </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=1v03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v03 OCA], [https://pdbe.org/1v03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v03 RCSB], [https://www.ebi.ac.uk/pdbsum/1v03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v03 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=1v03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v03 OCA], [https://pdbe.org/1v03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v03 RCSB], [https://www.ebi.ac.uk/pdbsum/1v03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v03 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q41290_SORBI Q41290_SORBI] |
| | == 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: Andropogon sorghum]] | |
| - | [[Category: Beta-glucosidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bevan, D R]] | + | [[Category: Sorghum bicolor]] |
| - | [[Category: Czjzek, M]] | + | [[Category: Bevan DR]] |
| - | [[Category: Esen, A]] | + | [[Category: Czjzek M]] |
| - | [[Category: Henrissat, B]] | + | [[Category: Esen A]] |
| - | [[Category: Moriniere, J]] | + | [[Category: Henrissat B]] |
| - | [[Category: Verdoucq, L]] | + | [[Category: Moriniere J]] |
| - | [[Category: Dhurrin hydrolysis]]
| + | [[Category: Verdoucq L]] |
| - | [[Category: Family gh1]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Pest defense]]
| + | |
| Structural highlights
Function
Q41290_SORBI
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
Plant beta-glucosidases play a crucial role in defense against pests. They cleave, with variable specificity, beta-glucosides to release toxic aglycone moieties. The Sorghum bicolor beta-glucosidase isoenzyme Dhr1 has a strict specificity for its natural substrate dhurrin (p-hydroxy-(S)-mandelonitrile-beta-D-glucoside), whereas its close homolog, the maize beta-glucosidase isoenzyme Glu1, which shares 72% sequence identity, hydrolyzes a broad spectrum of substrates in addition to its natural substrate 2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxaxin-3-one. Structural data from enzyme.substrate complexes of Dhr1 show that the mode of aglycone binding differs from that previously observed in the homologous maize enzyme. Specifically, the data suggest that Asn(259), Phe(261), and Ser(462), located in the aglycone-binding site of S. bicolor Dhr1, are crucial for aglycone recognition and binding. The tight binding of the aglycone moiety of dhurrin promotes the stabilization of the reaction intermediate in which the glycone moiety is in a deformed (1)S(3) conformation within the glycone-binding site, ready for nucleophilic attack to occur. Compared with the broad specificity maize beta-glucosidase, this different binding mode explains the narrow specificity of sorghum dhurrinase-1.
Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate.,Verdoucq L, Moriniere J, Bevan DR, Esen A, Vasella A, Henrissat B, Czjze M J Biol Chem. 2004 Jul 23;279(30):31796-803. Epub 2004 May 17. PMID:15148317[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Verdoucq L, Moriniere J, Bevan DR, Esen A, Vasella A, Henrissat B, Czjze M. Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate. J Biol Chem. 2004 Jul 23;279(30):31796-803. Epub 2004 May 17. PMID:15148317 doi:10.1074/jbc.M402918200
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