6GGL
Crystal structure of CotB2 variant F107A
Summary for 6GGL
| Entry DOI | 10.2210/pdb6ggl/pdb |
| Descriptor | Cyclooctat-9-en-7-ol synthase, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | terpene synthase, cyclooctatin, lyase |
| Biological source | Streptomyces melanosporofaciens |
| Total number of polymer chains | 2 |
| Total formula weight | 73472.91 |
| Authors | Driller, R.,Janke, S.,Fuchs, M.,Warner, E.,Mhashal, A.R.,Major, D.T.,Christmann, M.,Brueck, T.,Loll, B. (deposition date: 2018-05-03, release date: 2018-10-10, Last modification date: 2024-01-17) |
| Primary citation | Driller, R.,Janke, S.,Fuchs, M.,Warner, E.,Mhashal, A.R.,Major, D.T.,Christmann, M.,Bruck, T.,Loll, B. Towards a comprehensive understanding of the structural dynamics of a bacterial diterpene synthase during catalysis. Nat Commun, 9:3971-3971, 2018 Cited by PubMed Abstract: Terpenes constitute the largest and structurally most diverse natural product family. Most terpenoids exhibit a stereochemically complex macrocyclic core, which is generated by C-C bond forming of aliphatic oligo-prenyl precursors. This reaction is catalysed by terpene synthases (TPSs), which are capable of chaperoning highly reactive carbocation intermediates through an enzyme-specific reaction. Due to the instability of carbocation intermediates, the proteins' structural dynamics and enzyme:substrate interactions during TPS catalysis remain elusive. Here, we present the structure of the diterpene synthase CotB2, in complex with an in crystallo cyclised abrupt reaction product and a substrate-derived diphosphate. We captured additional snapshots of the reaction to gain an overview of CotB2's catalytic mechanism. To enhance insights into catalysis, structural information is augmented with multiscale molecular dynamic simulations. Our data represent fundamental TPS structure dynamics during catalysis, which ultimately enable rational engineering towards tailored terpene macrocycles that are inaccessible by conventional chemical synthesis. PubMed: 30266969DOI: 10.1038/s41467-018-06325-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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