5UV0

Crystal Structure of (+)-Limonene Synthase from Citrus sinensis

5UV0 の概要

• エントリーDOI: 10.2210/pdb5uv0/pdb
• 関連するPDBエントリー: 5UV1 5UV2
• 分子名称: (+)-limonene synthase (2 entities in total)
• 機能のキーワード: terpene synthase, enantiomer, terpene synthase fold, monoterpene, lyase
• 由来する生物種: Citrus sinensis (Sweet orange)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 70441.22

構造登録者

Prem Kumar, R.,Oprian, D.D. (登録日: 2017-02-17, 公開日: 2017-03-22, 最終更新日: 2023-10-04)

主引用文献

Morehouse, B.R.,Kumar, R.P.,Matos, J.O.,Olsen, S.N.,Entova, S.,Oprian, D.D.
Functional and Structural Characterization of a (+)-Limonene Synthase from Citrus sinensis.
Biochemistry, 56:1706-1715, 2017

PubMed Abstract: Terpenes make up the largest and most diverse class of natural compounds and have important commercial and medical applications. Limonene is a cyclic monoterpene (C) present in nature as two enantiomers, (+) and (-), which are produced by different enzymes. The mechanism of production of the (-)-enantiomer has been studied in great detail, but to understand how enantiomeric selectivity is achieved in this class of enzymes, it is important to develop a thorough biochemical description of enzymes that generate (+)-limonene, as well. Here we report the first cloning and biochemical characterization of a (+)-limonene synthase from navel orange (Citrus sinensis). The enzyme obeys classical Michaelis-Menten kinetics and produces exclusively the (+)-enantiomer. We have determined the crystal structure of the apoprotein in an "open" conformation at 2.3 Å resolution. Comparison with the structure of (-)-limonene synthase (Mentha spicata), which is representative of a fully closed conformation (Protein Data Bank entry 2ONG ), reveals that the short H-α1 helix moves nearly 5 Å inward upon substrate binding, and a conserved Tyr flips to point its hydroxyl group into the active site.

PubMed: 28272875
DOI: 10.1021/acs.biochem.7b00143

実験手法

X-RAY DIFFRACTION (2.3 Å)