7Y50

Class I diterpene synthase (CyS) from Streptomyces cattleya

Summary for 7Y50

• Entry DOI: 10.2210/pdb7y50/pdb
• Descriptor: Putative glutamate dehydrogenase/leucine dehydrogenase (2 entities in total)
• Functional Keywords: class i diterpene synthase (cys) from streptomyces cattleya, biosynthetic protein
• Biological source: Streptomyces cattleya
• Total number of polymer chains: 1
• Total formula weight: 42050.56

Authors

Xing, B.,Ma, M. (deposition date: 2022-06-16, release date: 2022-12-21, Last modification date: 2023-11-29)

Primary citation

Xing, B.,Xu, H.,Li, A.,Lou, T.,Xu, M.,Wang, K.,Xu, Z.,Dickschat, J.S.,Yang, D.,Ma, M.
Crystal Structure Based Mutagenesis of Cattleyene Synthase Leads to the Generation of Rearranged Polycyclic Diterpenes.
Angew.Chem.Int.Ed.Engl., 61:e202209785-e202209785, 2022

PubMed Abstract: The crystal structures of cattleyene synthase (apo-CyS), and CyS complexed with geranylgeranyl pyrophosphate (GGPP) were solved. The CyS variant exhibited an increased production of cattleyene and other diterpenes with diverse skeletons. Its structure showed a widened active site cavity explaining the relaxed selectivity. Isotopic labeling experiments revealed a remarkable cyclization mechanism involving several skeletal rearrangements for one of the novel diterpenes.

PubMed: 35819825
DOI: 10.1002/anie.202209785

Experimental method

X-RAY DIFFRACTION (2 Å)