4.2 Article

CryoEM analysis of small plant biocatalysts at sub-2 Å resolution

Journal

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S205979832101216X

Keywords

cryo-electron microscopy; camphor; terpenes; borneol dehydrogenases; high resolution; green chemistry; plant biocatalysts

Funding

  1. German Federal Ministry of Education and Research (BMBF) [031B050B]
  2. Austrian Science Funds (FWF) [P31001-B29]
  3. Deutsche Forschungsgemeinschaft [HA 2549/15-2]
  4. Deutsche Forschungsgemeinschaft
  5. state of Berlin [INST 335/588-1 FUGG, INST 335/589-1 FUGG, INST 335/590-1 FUGG]
  6. Hanns Seidel Foundation
  7. Austrian Science Fund (FWF) [P31001] Funding Source: Austrian Science Fund (FWF)

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Enzyme catalysis is a crucial technology for developing efficient and sustainable processes. Plants provide diverse enzymes that facilitate complex reactions. Cryo-electron microscopy can reveal the structures of plant enzymes, providing a pathway for developing new biocatalysts.
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 similar to 120 kDa at or below 2 angstrom resolution, paving the way for the rapid development of new biocatalysts that can provide access to bioactive terpenes and terpenoids.

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