6v0k

Crystal structure of Penicillium verruculosum copalyl diphosphate synthase (PvCPS) alpha prenyltransferase domain

spinqualitylabelsall models 6v0k, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6v0k is a 2 chain structure with sequence from Talaromyces verruculosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.41Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PVCPS_TALVE Bifunctional terpene synthase that possesses both prenyltransferase and type II terpene cyclase activity, converting isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into geranylgeranyl diphosphate (GGPP) and further converting GGPP into copalyl diphosphate, respectively. Publication Abstract from PubMed The unusual diterpene (C20) synthase copalyl diphosphate synthase from Penicillium verruculosum (PvCPS) is the first bifunctional terpene synthase identified with both prenyltransferase and class II cyclase activities in a single polypeptide chain with alphabetagamma domain architecture. The C-terminal prenyltransferase alphadomain generates geranylgeranyl diphosphate which is then cyclized to form copalyl diphosphate at the N-terminal betagamma domain interface. We now demonstrate that PvCPS exists as a hexamer at high concentrations - a unique quaternary structure for known alphabetagamma terpene synthases. Hexamer assembly is corroborated by a 2.41 A-resolution crystal structure of the alpha domain prenyltransferase obtained from limited proteolysis of full-length PvCPS, as well as the ab initio modeling of full-length PvCPS derived from small-angle X-ray scattering data. Hexamerization of the prenyltransferase alphadomain appears to drive the hexamerization of full-length PvCPS. The PvCPS hexamer dissociates into lower-order species at lower concentrations, as evidenced by size-exclusion chromatography in-line with multiangle light scattering, sedimentation velocity analytical ultracentrifugation, and native polyacrylamide gel electrophoresis experiments, suggesting that oligomerization is concentration dependent. Even so, PvCPS oligomer assembly does not affect prenyltransferase activity in vitro. Higher-Order Oligomerization of a Chimeric alphabetagamma Bifunctional Diterpene Synthase with Prenyltransferase and Class II Cyclase Activities is Concentration-Dependent.,Ronnebaum TA, Gupta K, Christianson DW J Struct Biol. 2020 Jan 21:107463. doi: 10.1016/j.jsb.2020.107463. PMID:31978464 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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