4atd: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==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/Ophioxylon_serpentinum Ophioxylon serpentinum]. 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> | ||
| Line 25: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Ophioxylon serpentinum]] | ||
[[Category: Raucaffricine beta-glucosidase]] | [[Category: Raucaffricine beta-glucosidase]] | ||
[[Category: Panjikar, S]] | [[Category: Panjikar, S]] | ||
Revision as of 11:59, 6 March 2019
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
|
| ||||||||||||||||||||