5c05

Crystal Structure of Gamma-terpinene Synthase from Thymus vulgarisCrystal Structure of Gamma-terpinene Synthase from Thymus vulgaris

Structural highlights 5c05 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed The biosynthesis of gamma-terpinene, a precursor of the phenolic isomers thymol and carvacrol found in the essential oil from Thymus sp., is attributed to the activitiy of gamma-terpinene synthase (TPS). Purified gamma-terpinene synthase from T. vulgaris (TvTPS), the Thymus species that is the most widely spread and of the greatest economical importance, is able to catalyze the enzymatic conversion of geranyl diphosphate (GPP) to gamma-terpinene. The crystal structure of recombinantly expressed and purified TvTPS is reported at 1.65 A resolution, confirming the dimeric structure of the enzyme. The putative active site of TvTPS is deduced from its pronounced structural similarity to enzymes from other species of the Lamiaceae family involved in terpenoid biosynthesis: to (+)-bornyl diphosphate synthase and 1,8-cineole synthase from Salvia sp. and to (4S)-limonene synthase from Mentha spicata. Expression, crystallization and structure elucidation of gamma-terpinene synthase from Thymus vulgaris.,Rudolph K, Parthier C, Egerer-Sieber C, Geiger D, Muller YA, Kreis W, Muller-Uri F Acta Crystallogr F Struct Biol Commun. 2016 Jan 1;72(Pt 1):16-23. doi:, 10.1107/S2053230X15023043. Epub 2016 Jan 1. PMID:26750479 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 5c05, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image