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| | ==Rice Os3BGlu6 Beta-Glucosidase E178Q mutant in a covalent complex with Glc from GA4GE.== | | ==Rice Os3BGlu6 Beta-Glucosidase E178Q mutant in a covalent complex with Glc from GA4GE.== |
| - | <StructureSection load='3wbe' size='340' side='right' caption='[[3wbe]], [[Resolution|resolution]] 1.97Å' scene=''> | + | <StructureSection load='3wbe' size='340' side='right'caption='[[3wbe]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wbe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Japanese_rice Japanese rice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WBE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wbe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WBE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.97Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wba|3wba]], [[3gnp|3gnp]], [[3gnr|3gnr]], [[3gno|3gno]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BGLU6, LOC_Os03g11420, Os03g0212800 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Japanese rice])</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=3wbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wbe OCA], [https://pdbe.org/3wbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wbe RCSB], [https://www.ebi.ac.uk/pdbsum/3wbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wbe ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wbe OCA], [http://pdbe.org/3wbe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wbe RCSB], [http://www.ebi.ac.uk/pdbsum/3wbe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wbe ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BGL06_ORYSJ BGL06_ORYSJ]] Hydrolyzes glycosides, oligosaccharides and hydrophobic glycosides. | + | [https://www.uniprot.org/uniprot/BGL06_ORYSJ BGL06_ORYSJ] Hydrolyzes glycosides, oligosaccharides and hydrophobic glycosides. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Beta-glucosidase|Beta-glucosidase]] | + | *[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-glucosidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Japanese rice]] | + | [[Category: Oryza sativa Japonica Group]] |
| - | [[Category: Cairns, J R.K]] | + | [[Category: Cairns JRK]] |
| - | [[Category: Hua, Y]] | + | [[Category: Hua Y]] |
| - | [[Category: Sansenya, S]] | + | [[Category: Sansenya S]] |
| - | [[Category: Beta-d-glucosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Tim barrel]]
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| Structural highlights
Function
BGL06_ORYSJ Hydrolyzes glycosides, oligosaccharides and hydrophobic glycosides.
Publication Abstract from PubMed
In order to identify a rice gibberellin ester beta-d-glucosidase, gibberellin A4 beta-d-glucosyl ester (GA4-GE) was synthesized and used to screen rice beta-glucosidases. Os3BGlu6 was found to have the highest hydrolysis activity to GA4-GE among five recombinantly expressed rice glycoside hydrolase family GH1 enzymes from different phylogenic clusters. The kinetic parameters of Os3BGlu6 and its mutants E178Q, E178A, E394D, E394Q and M251N for hydrolysis of p-nitrophenyl beta-d-glucopyranoside (pNPGlc) and GA4-GE confirmed the roles of the catalytic acid/base and nucleophile for hydrolysis of both substrates and suggested M251 contributes to binding hydrophobic aglycones. The activities of the Os3BGlu6 E178Q and E178A acid/base mutants were rescued by azide, which they transglucosylate to produce beta-d-glucopyranosyl azide, in a pH-dependent manner, while acetate also rescued Os3BGlu6 E178A at low pH. High concentrations of sodium azide (200-400mM) inhibited Os3BGlu6 E178Q but not Os3BGlu6 E178A. The structures of Os3BGlu6 E178Q crystallized with either GA4-GE or pNPGlc had a native alpha-d-glucosyl moiety covalently linked to the catalytic nucleophile, E394, which showed the hydrogen bonding to the 2-hydroxyl in the covalent intermediate. These data suggest that a GH1 beta-glucosidase uses the same retaining catalytic mechanism to hydrolyze 1-O-acyl glucose ester and glucoside.
Enzymatic and structural characterization of hydrolysis of gibberellin A4 glucosyl ester by a rice beta-d-glucosidase.,Hua Y, Sansenya S, Saetang C, Wakuta S, Ketudat Cairns JR Arch Biochem Biophys. 2013 Sep 1;537(1):39-48. doi: 10.1016/j.abb.2013.06.005., Epub 2013 Jun 26. PMID:23811195[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hua Y, Sansenya S, Saetang C, Wakuta S, Ketudat Cairns JR. Enzymatic and structural characterization of hydrolysis of gibberellin A4 glucosyl ester by a rice beta-d-glucosidase. Arch Biochem Biophys. 2013 Sep 1;537(1):39-48. doi: 10.1016/j.abb.2013.06.005., Epub 2013 Jun 26. PMID:23811195 doi:10.1016/j.abb.2013.06.005
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