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3wq5
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==beta-Primeverosidase in complex with disaccharide substrate-analog N-beta-primeverosylamidine, natural aglycone derivative== | ==beta-Primeverosidase in complex with disaccharide substrate-analog N-beta-primeverosylamidine, natural aglycone derivative== | ||
| - | <StructureSection load='3wq5' size='340' side='right' caption='[[3wq5]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3wq5' size='340' side='right'caption='[[3wq5]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3wq5]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3wq5]] 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=3WQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WQ5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=VPA:2-PHENYL-N-(6-O-BETA-D-XYLOPYRANOSYL-BETA-D-GLUCOPYRANOSYL)ETHYLAMIDINE'>VPA</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=VPA:2-PHENYL-N-(6-O-BETA-D-XYLOPYRANOSYL-BETA-D-GLUCOPYRANOSYL)ETHYLAMIDINE'>VPA</scene></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=3wq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wq5 OCA], [https://pdbe.org/3wq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wq5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wq5 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q7X9A9_CAMSI Q7X9A9_CAMSI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:24753293</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3wq5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Camellia sinensis]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Saino | + | [[Category: Saino H]] |
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Current revision
beta-Primeverosidase in complex with disaccharide substrate-analog N-beta-primeverosylamidine, natural aglycone derivative
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