6V0K

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

6V0K の概要

• エントリーDOI: 10.2210/pdb6v0k/pdb
• 分子名称: Terpene synthase, GLYCEROL (3 entities in total)
• 機能のキーワード: isoprenoid synthase, prenyltransferase, transferase
• 由来する生物種: Talaromyces verruculosus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69760.03

構造登録者

Christianson, D.W.,Ronnebaum, T.A. (登録日: 2019-11-18, 公開日: 2020-01-29, 最終更新日: 2023-10-11)

主引用文献

Ronnebaum, T.A.,Gupta, K.,Christianson, D.W.
Higher-order oligomerization of a chimeric alpha beta gamma bifunctional diterpene synthase with prenyltransferase and class II cyclase activities is concentration-dependent.
J.Struct.Biol., 210:107463-107463, 2020

PubMed Abstract: The unusual diterpene (C) 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 αβγ domain architecture. The C-terminal prenyltransferase α domain generates geranylgeranyl diphosphate which is then cyclized to form copalyl diphosphate at the N-terminal βγ domain interface. We now demonstrate that PvCPS exists as a hexamer at high concentrations - a unique quaternary structure for known αβγ terpene synthases. Hexamer assembly is corroborated by a 2.41 Å-resolution crystal structure of the α domain prenyltransferase obtained from limited proteolysis of full-length PvCPS, as well as the ab initio model of full-length PvCPS derived from small-angle X-ray scattering data. Hexamerization of the prenyltransferase α domain 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.

PubMed: 31978464
DOI: 10.1016/j.jsb.2020.107463

実験手法

X-RAY DIFFRACTION (2.41 Å)