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2JF7

Structure of Strictosidine Glucosidase

2JF7 の概要
エントリーDOI10.2210/pdb2jf7/pdb
関連するPDBエントリー2JF6
分子名称STRICTOSIDINE-O-BETA-D-GLUCOSIDASE (2 entities in total)
機能のキーワードalkaloid, glucosidase, strictosidine, 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121918.80
構造登録者
Barleben, L.,Panjikar, S.,Ruppert, M.,Koepke, J.,Stockigt, J. (登録日: 2007-01-26, 公開日: 2008-02-05, 最終更新日: 2023-12-13)
主引用文献Barleben, L.,Panjikar, S.,Ruppert, M.,Koepke, J.,Stockigt, J.
Molecular Architecture of Strictosidine Glucosidase - the Gateway to the Biosynthesis of the Monoterpenoid Indole Alkaloid Family
Plant Cell, 19:2886-, 2007
Cited by
PubMed Abstract: Strictosidine beta-D-glucosidase (SG) follows strictosidine synthase (STR1) in the production of the reactive intermediate required for the formation of the large family of monoterpenoid indole alkaloids in plants. This family is composed of approximately 2000 structurally diverse compounds. SG plays an important role in the plant cell by activating the glucoside strictosidine and allowing it to enter the multiple indole alkaloid pathways. Here, we report detailed three-dimensional information describing both native SG and the complex of its inactive mutant Glu207Gln with the substrate strictosidine, thus providing a structural characterization of substrate binding and identifying the amino acids that occupy the active site surface of the enzyme. Structural analysis and site-directed mutagenesis experiments demonstrate the essential role of Glu-207, Glu-416, His-161, and Trp-388 in catalysis. Comparison of the catalytic pocket of SG with that of other plant glucosidases demonstrates the structural importance of Trp-388. Compared with all other glucosidases of plant, bacterial, and archaeal origin, SG's residue Trp-388 is present in a unique structural conformation that is specific to the SG enzyme. In addition to STR1 and vinorine synthase, SG represents the third structural example of enzymes participating in the biosynthetic pathway of the Rauvolfia alkaloid ajmaline. The data presented here will contribute to deciphering the structure and reaction mechanism of other higher plant glucosidases.
PubMed: 17890378
DOI: 10.1105/TPC.106.045682
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.48 Å)
構造検証レポート
Validation report summary of 2jf7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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