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-Structure paper
タイトル | CryoEM analysis of small plant biocatalysts at sub-2 Å resolution. |
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ジャーナル・号・ページ | Acta Crystallogr D Struct Biol, Vol. 78, Issue Pt 1, Page 113-123, Year 2022 |
掲載日 | 2022年1月1日 |
著者 | Nicole Dimos / Carl P O Helmer / Andrea M Chánique / Markus C Wahl / Robert Kourist / Tarek Hilal / Bernhard Loll / |
PubMed 要旨 | Enzyme catalysis has emerged as a key technology for developing efficient, sustainable processes in the chemical, biotechnological and pharmaceutical industries. Plants provide large and diverse ...Enzyme catalysis has emerged as a key technology for developing efficient, sustainable processes in the chemical, biotechnological and pharmaceutical industries. Plants provide large and diverse pools of biosynthetic enzymes that facilitate complex reactions, such as the formation of intricate terpene carbon skeletons, with exquisite specificity. High-resolution structural analysis of these enzymes is crucial in order to understand their mechanisms and modulate their properties by targeted engineering. Although cryo-electron microscopy (cryoEM) has revolutionized structural biology, its applicability to high-resolution structural analysis of comparatively small enzymes has so far been largely unexplored. Here, it is shown that cryoEM can reveal the structures of plant borneol dehydrogenases of ∼120 kDa at or below 2 Å resolution, paving the way for the rapid development of new biocatalysts that can provide access to bioactive terpenes and terpenoids. |
リンク | Acta Crystallogr D Struct Biol / PubMed:34981767 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 1.88 - 2.04 Å |
構造データ | EMDB-12739, PDB-7o6p: EMDB-12740, PDB-7o6q: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | OXIDOREDUCTASE / TERPENOID / ALCOHOL / BORNEOL / ROSSMANN-LIKE FOLD |