7o6p | pdb_00007o6p

Structure of the borneol dehydrogenase 2 of Salvia officinalis

spinqualitylabelsall models 7o6p, resolution 2.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7o6p is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 approximately 120 kDa at or below 2 A resolution, paving the way for the rapid development of new biocatalysts that can provide access to bioactive terpenes and terpenoids. CryoEM analysis of small plant biocatalysts at sub-2 A resolution.,Dimos N, Helmer CPO, Chanique AM, Wahl MC, Kourist R, Hilal T, Loll B Acta Crystallogr D Struct Biol. 2022 Jan 1;78(Pt 1):113-123. doi:, 10.1107/S205979832101216X. Epub 2022 Jan 1. PMID:34981767 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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