7XKX

Crystal structure of Tpn2

Summary for 7XKX

• Entry DOI: 10.2210/pdb7xkx/pdb
• Descriptor: SQHop_cyclase_C domain-containing protein (2 entities in total)
• Functional Keywords: tpn2, terpene synthase, terpentecin, bacterial ts, biosynthetic protein
• Biological source: Kitasatospora sp. CB02891
• Total number of polymer chains: 2
• Total formula weight: 116043.28

Authors

Chang, C.Y.,Stowell, E.A.,Lin, Y.L.,Ehrenberger, M.A.,Rudolf, J.D. (deposition date: 2022-04-20, release date: 2023-03-01, Last modification date: 2023-11-29)

Primary citation

Stowell, E.A.,Ehrenberger, M.A.,Lin, Y.L.,Chang, C.Y.,Rudolf, J.D.
Structure-guided product determination of the bacterial type II diterpene synthase Tpn2.
Commun Chem, 5:146-146, 2022

PubMed Abstract: A grand challenge in terpene synthase (TS) enzymology is the ability to predict function from protein sequence. Given the limited number of characterized bacterial TSs and significant sequence diversities between them and their eukaryotic counterparts, this is currently impossible. To contribute towards understanding the sequence-structure-function relationships of type II bacterial TSs, we determined the structure of the terpentedienyl diphosphate synthase Tpn2 from Kitasatospora sp. CB02891 by X-ray crystallography and made structure-guided mutants to probe its mechanism. Substitution of a glycine into a basic residue changed the product preference from the clerodane skeleton to a syn-labdane skeleton, resulting in the first syn-labdane identified from a bacterial TS. Understanding how a single residue can dictate the cyclization pattern in Tpn2, along with detailed bioinformatics analysis of bacterial type II TSs, sets the stage for the investigation of the functional scope of bacterial type II TSs and the discovery of novel bacterial terpenoids.

PubMed: 36698006
DOI: 10.1038/s42004-022-00765-6

Experimental method

X-RAY DIFFRACTION (2.57 Å)