4ATD

Crystal structure of native Raucaffricine glucosidase

4ATD の概要

• エントリーDOI: 10.2210/pdb4atd/pdb
• 関連するPDBエントリー: 4A3Y
• 分子名称: RAUCAFFRICINE-O-BETA-D-GLUCOSIDASE, SULFATE ION (3 entities in total)
• 機能のキーワード: alkaloid, hydrolase
• 由来する生物種: RAUVOLFIA SERPENTINA (SERPENTWOOD)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116144.99

構造登録者

Xia, L.,Rajendran, C.,Ruppert, M.,Panjikar, S.,Wang, M.,Stoeckigt, J. (登録日: 2012-05-05, 公開日: 2013-01-16, 最終更新日: 2023-12-20)

主引用文献

Xia, L.,Rajendran, C.,Ruppert, M.,Panjikar, S.,Wang, M.,Stoeckigt, J.
High Speed X-Ray Analysis of Plant Enzymes at Room Temperature
Phytochemistry, 91:88-, 2013

PubMed Abstract: X-ray measurements at room temperature (295 K) deliver high quality data sets with unprecedented speed (<2 min), as shown for crystallized raucaffricine-O-β-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.

PubMed: 22704651
DOI: 10.1016/J.PHYTOCHEM.2012.05.009

実験手法

X-RAY DIFFRACTION (2.1 Å)