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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]] 2.10&Aring;' scene=''>
<StructureSection load='4atd' size='340' side='right'caption='[[4atd]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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='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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a3y|4a3y]]</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='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'>[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>
<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>
== 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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Beta-glucosidase|Beta-glucosidase]]
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Devilpepper]]
[[Category: Large Structures]]
[[Category: Raucaffricine beta-glucosidase]]
[[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: Hydrolase]]

Latest revision as of 14:35, 20 December 2023

Crystal structure of native Raucaffricine glucosidaseCrystal structure of native Raucaffricine glucosidase

Structural highlights

4atd is a 2 chain structure with sequence from Rauvolfia serpentina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Warzecha H, Gerasimenko I, Kutchan TM, Stockigt J. Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis. Phytochemistry. 2000 Aug;54(7):657-66. doi: 10.1016/s0031-9422(00)00175-8. PMID:10975500 doi:http://dx.doi.org/10.1016/s0031-9422(00)00175-8
  2. Xia L, Rajendran C, Ruppert M, Panjikar S, Wang M, Stoeckigt J. High speed X-ray analysis of plant enzymes at room temperature. Phytochemistry. 2012 Jun 13. PMID:22704651 doi:10.1016/j.phytochem.2012.05.009

4atd, resolution 2.10Å

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