5HC8

Crystal structure of lavandulyl diphosphate synthase from Lavandula x intermedia in complex with dimethylallyl diphosphate

5HC8 の概要

• エントリーDOI: 10.2210/pdb5hc8/pdb
• 関連するPDBエントリー: 5HC6 5HC7
• 分子名称: prenyltransference for protein, MAGNESIUM ION, TRIHYDROGEN THIODIPHOSPHATE, ... (7 entities in total)
• 機能のキーワード: substrate binding, prenyltransferase, substrate, transferase
• 由来する生物種: Lavandula lanata
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30395.33

構造登録者

Liu, M.X.,Liu, W.D.,Gao, J.,Zheng, Y.Y.,Chen, C.C.,Guo, R.T. (登録日: 2016-01-04, 公開日: 2016-03-02, 最終更新日: 2023-11-08)

主引用文献

Liu, M.X.,Chen, C.C.,Chen, L.,Xiao, X.S.,Zheng, Y.Y.,Huang, J.W.,Liu, W.d.,Ko, T.P.,Cheng, Y.S.,Feng, X.X.,Oldfield, E.,Guo, R.T.,Ma, Y.H.
Structure and Function of a "Head-to-Middle" Prenyltransferase: Lavandulyl Diphosphate Synthase
Angew.Chem.Int.Ed.Engl., 55:4721-4724, 2016

PubMed Abstract: We report the first X-ray structure of the unique "head-to-middle" monoterpene synthase, lavandulyl diphosphate synthase (LPPS). LPPS catalyzes the condensation of two molecules of dimethylallyl diphosphate (DMAPP) to form lavandulyl diphosphate, a precursor to the fragrance lavandulol. The structure is similar to that of the bacterial cis-prenyl synthase, undecaprenyl diphosphate synthase (UPPS), and contains an allylic site (S1) in which DMAPP ionizes and a second site (S2) which houses the DMAPP nucleophile. Both S-thiolo-dimethylallyl diphosphate and S-thiolo-isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 (Asn in UPPS) is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product. The results are of interest since they provide the first structure and structure-based mechanism of this unusual prenyl synthase.

PubMed: 26922900
DOI: 10.1002/anie.201600656

実験手法

X-RAY DIFFRACTION (1.87 Å)