5UV0
Crystal Structure of (+)-Limonene Synthase from Citrus sinensis
Summary for 5UV0
| Entry DOI | 10.2210/pdb5uv0/pdb |
| Related | 5UV1 5UV2 |
| Descriptor | (+)-limonene synthase (2 entities in total) |
| Functional Keywords | terpene synthase, enantiomer, terpene synthase fold, monoterpene, lyase |
| Biological source | Citrus sinensis (Sweet orange) |
| Total number of polymer chains | 1 |
| Total formula weight | 70441.22 |
| Authors | Prem Kumar, R.,Oprian, D.D. (deposition date: 2017-02-17, release date: 2017-03-22, Last modification date: 2023-10-04) |
| Primary citation | 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 Cited by 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: 28272875DOI: 10.1021/acs.biochem.7b00143 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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