7O6Q
Structure of the borneol dehydrogenase 1 of salvia rosmarinus
Summary for 7O6Q
| Entry DOI | 10.2210/pdb7o6q/pdb |
| EMDB information | 12740 |
| Descriptor | borneol dehydrogenase (2 entities in total) |
| Functional Keywords | terpenoid, alcohol, oxidoreductase, borneol, rossmann-like fold |
| Biological source | Salvia rosmarinus |
| Total number of polymer chains | 4 |
| Total formula weight | 121138.12 |
| Authors | Dimos, N.,Helmer, C.P.O.,Hilal, T.,Loll, B. (deposition date: 2021-04-12, release date: 2021-12-01, Last modification date: 2024-07-10) |
| Primary citation | Dimos, N.,Helmer, C.P.O.,Chanique, A.M.,Wahl, M.C.,Kourist, R.,Hilal, T.,Loll, B. CryoEM analysis of small plant biocatalysts at sub-2 angstrom resolution. Acta Crystallogr D Struct Biol, 78:113-123, 2022 Cited by PubMed Abstract: 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. PubMed: 34981767DOI: 10.1107/S205979832101216X PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.88 Å) |
Structure validation
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