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==Crystal structure of native Raucaffricine glucosidase== | ==Crystal structure of native Raucaffricine glucosidase== | ||
<StructureSection load='4atd' size='340' side='right' caption='[[4atd]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4atd' size='340' side='right' caption='[[4atd]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4atd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4atd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Devilpepper Devilpepper]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ATD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a3y|4a3y]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a3y|4a3y]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Raucaffricine_beta-glucosidase Raucaffricine beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.125 3.2.1.125] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Raucaffricine_beta-glucosidase Raucaffricine beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.125 3.2.1.125] </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=4atd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4atd RCSB], [http://www.ebi.ac.uk/pdbsum/4atd PDBsum]</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=4atd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atd OCA], [http://pdbe.org/4atd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4atd RCSB], [http://www.ebi.ac.uk/pdbsum/4atd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4atd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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 4atd" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Devilpepper]] | |||
[[Category: Raucaffricine beta-glucosidase]] | [[Category: Raucaffricine beta-glucosidase]] | ||
[[Category: Panjikar, S]] | [[Category: Panjikar, S]] | ||
[[Category: Rajendran, C]] | [[Category: Rajendran, C]] | ||
Revision as of 09:59, 5 August 2016
Crystal structure of native Raucaffricine glucosidaseCrystal structure of native Raucaffricine glucosidase
Structural highlights
Publication Abstract from PubMedX-ray measurements at room temperature (295K) deliver high quality data sets with unprecedented speed (<2min), as shown for crystallized raucaffricine-O-beta-d-glucosidase (RG), its mutant RG-Glu186Gln and several ligand complexes of the enzyme which participates in alkaloid biosynthesis in the plant Rauvolfia. The data obtained are compared with data sets measured under typical cryo conditions (100K). Under both conditions, density maps are highly comparable and favor the described protocol for room temperature measurements, potentially paving the way for future crystallographic studies capturing biosynthetic pathway intermediates. High speed X-ray analysis of plant enzymes at room temperature.,Xia L, Rajendran C, Ruppert M, Panjikar S, Wang M, Stoeckigt J Phytochemistry. 2012 Jun 13. PMID:22704651[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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