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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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4ATD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4atd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atd OCA], [https://pdbe.org/4atd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4atd RCSB], [https://www.ebi.ac.uk/pdbsum/4atd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4atd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RG1_RAUSE RG1_RAUSE] Glucosidase specifically involved in alkaloid biosynthesis leading to the accumulation of several alkaloids, including ajmaline, an important plant-derived pharmaceutical used in the treatment of heart disorders.<ref>PMID:10975500</ref> | |||
<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> | |||
<div class="pdbe-citations 4atd" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Rauvolfia serpentina]] | [[Category: Rauvolfia serpentina]] | ||
[[Category: Panjikar | [[Category: Panjikar S]] | ||
[[Category: Rajendran | [[Category: Rajendran C]] | ||
[[Category: Ruppert | [[Category: Ruppert M]] | ||
[[Category: Stoeckigt | [[Category: Stoeckigt J]] | ||
[[Category: Wang | [[Category: Wang M]] | ||
[[Category: Xia | [[Category: Xia L]] | ||
Latest revision as of 14:35, 20 December 2023
Crystal structure of native Raucaffricine glucosidaseCrystal structure of native Raucaffricine glucosidase
Structural highlights
FunctionRG1_RAUSE Glucosidase specifically involved in alkaloid biosynthesis leading to the accumulation of several alkaloids, including ajmaline, an important plant-derived pharmaceutical used in the treatment of heart disorders.[1] 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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