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| | ==Crystal structure of beta-primeverosidase== | | ==Crystal structure of beta-primeverosidase== |
| - | <StructureSection load='3wq4' size='340' side='right' caption='[[3wq4]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3wq4' size='340' side='right'caption='[[3wq4]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wq4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Camsi Camsi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WQ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WQ4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wq4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Camellia_sinensis Camellia sinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WQ4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wq5|3wq5]], [[3wq6|3wq6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-primeverosidase Beta-primeverosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.149 3.2.1.149] </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=3wq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wq4 OCA], [https://pdbe.org/3wq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wq4 RCSB], [https://www.ebi.ac.uk/pdbsum/3wq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wq4 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=3wq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wq4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wq4 RCSB], [http://www.ebi.ac.uk/pdbsum/3wq4 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7X9A9_CAMSI Q7X9A9_CAMSI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3wq4" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-primeverosidase]] | + | [[Category: Camellia sinensis]] |
| - | [[Category: Camsi]] | + | [[Category: Large Structures]] |
| - | [[Category: Saino, H]] | + | [[Category: Saino H]] |
| - | [[Category: Aroma formation]]
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| - | [[Category: Black tea]]
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| - | [[Category: Diglycosidase]]
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| - | [[Category: Diglycoside]]
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| - | [[Category: Disaccharide]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Oolong tea]]
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| - | [[Category: Specific hydrolysis of beta-primeveroside]]
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| Structural highlights
Function
Q7X9A9_CAMSI
Publication Abstract from PubMed
beta-Primeverosidase (PD) is a disaccharide-specific beta-glycosidase in tea leaves. This enzyme is involved in aroma formation during the manufacturing process of oolong tea and black tea. PD hydrolyzes beta-primeveroside (6-O-beta-d-xylopyranosyl-beta-d-glucopyranoside) at the beta-glycosidic bond of primeverose to aglycone, and releases aromatic alcoholic volatiles of aglycones. PD only accepts primeverose as the glycone substrate, but broadly accepts various aglycones, including 2-phenylethanol, benzyl alcohol, linalool, and geraniol. We determined the crystal structure of PD complexes using highly specific disaccharide amidine inhibitors, N-beta-primeverosylamidines, and revealed the architecture of the active site responsible for substrate specificity. We identified three subsites in the active site: subsite -2 specific for 6-O-beta-d-xylopyranosyl, subsite -1 well conserved among beta-glucosidases and specific for beta-d-glucopyranosyl, and wide subsite +1 for hydrophobic aglycone. Glu-470, Ser-473, and Gln-477 act as the specific hydrogen bond donors for 6-O-beta-d-xylopyranosyl in subsite -2. On the other hand, subsite +1 was a large hydrophobic cavity that accommodates various aromatic aglycones. Compared with aglycone-specific beta-glucosidases of the glycoside hydrolase family 1, PD lacks the Trp crucial for aglycone recognition, and the resultant large cavity accepts aglycone and 6-O-beta-d-xylopyranosyl together. PD recognizes the beta-primeverosides in subsites -1 and -2 by hydrogen bonds, whereas the large subsite +1 loosely accommodates various aglycones. The glycone-specific activity of PD for broad aglycone substrates results in selective and multiple release of temporally stored alcoholic volatile aglycones of beta-primeveroside.
Crystal structures of beta-primeverosidase in complex with disaccharide amidine inhibitors.,Saino H, Shimizu T, Hiratake J, Nakatsu T, Kato H, Sakata K, Mizutani M J Biol Chem. 2014 Jun 13;289(24):16826-34. doi: 10.1074/jbc.M114.553271. Epub, 2014 Apr 21. PMID:24753293[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Saino H, Shimizu T, Hiratake J, Nakatsu T, Kato H, Sakata K, Mizutani M. Crystal structures of beta-primeverosidase in complex with disaccharide amidine inhibitors. J Biol Chem. 2014 Jun 13;289(24):16826-34. doi: 10.1074/jbc.M114.553271. Epub, 2014 Apr 21. PMID:24753293 doi:http://dx.doi.org/10.1074/jbc.M114.553271
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