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==Crystal structure of native Raucaffricine glucosidase== | |||
=== | <StructureSection load='4atd' size='340' side='right' caption='[[4atd]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4atd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rauvolfia_serpentina Rauvolfia serpentina]. 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> | |||
<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='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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
X-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<ref>PMID:22704651</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[Beta-glucosidase|Beta-glucosidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Raucaffricine beta-glucosidase]] | [[Category: Raucaffricine beta-glucosidase]] | ||
[[Category: Rauvolfia serpentina]] | [[Category: Rauvolfia serpentina]] | ||
[[Category: Panjikar, S | [[Category: Panjikar, S]] | ||
[[Category: Rajendran, C | [[Category: Rajendran, C]] | ||
[[Category: Ruppert, M | [[Category: Ruppert, M]] | ||
[[Category: Stoeckigt, J | [[Category: Stoeckigt, J]] | ||
[[Category: Wang, M | [[Category: Wang, M]] | ||
[[Category: Xia, L | [[Category: Xia, L]] | ||
[[Category: Alkaloid]] | [[Category: Alkaloid]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 12:11, 21 December 2014
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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