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| | <StructureSection load='5uv0' size='340' side='right'caption='[[5uv0]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5uv0' size='340' side='right'caption='[[5uv0]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uv0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Citsi Citsi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UV0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UV0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uv0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrus_sinensis Citrus sinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UV0 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uv2|5uv2]], [[5uv1|5uv1]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5uv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uv0 OCA], [http://pdbe.org/5uv0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uv0 RCSB], [http://www.ebi.ac.uk/pdbsum/5uv0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uv0 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5uv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uv0 OCA], [https://pdbe.org/5uv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uv0 RCSB], [https://www.ebi.ac.uk/pdbsum/5uv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uv0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/RLC1_CITSI RLC1_CITSI] Catalyzes the conversion of geranyl diphosphate to (+)-(4R)-limonene (PubMed:28272875, PubMed:28272876). Produces exclusively the (+)-enantiomer (PubMed:28272875). Can use neryl diphosphate as substrate (PubMed:28272876). Has no activity with farnesyl diphosphate (PubMed:28272875).<ref>PMID:28272875</ref> <ref>PMID:28272876</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Citsi]] | + | [[Category: Citrus sinensis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kumar, R Prem]]
| + | [[Category: Oprian DD]] |
| - | [[Category: Oprian, D D]] | + | [[Category: Prem Kumar R]] |
| - | [[Category: Enantiomer]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Monoterpene]]
| + | |
| - | [[Category: Terpene synthase]]
| + | |
| - | [[Category: Terpene synthase fold]]
| + | |
| Structural highlights
Function
RLC1_CITSI Catalyzes the conversion of geranyl diphosphate to (+)-(4R)-limonene (PubMed:28272875, PubMed:28272876). Produces exclusively the (+)-enantiomer (PubMed:28272875). Can use neryl diphosphate as substrate (PubMed:28272876). Has no activity with farnesyl diphosphate (PubMed:28272875).[1] [2]
Publication Abstract from PubMed
Terpenes make up the largest and most diverse class of natural compounds and have important commercial and medical applications. Limonene is a cyclic monoterpene (C10) 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 A 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-alpha1 helix moves nearly 5 A inward upon substrate binding, and a conserved Tyr flips to point its hydroxyl group into the active site.
Functional and Structural Characterization of a (+)-Limonene Synthase from Citrus sinensis.,Morehouse BR, Kumar RP, Matos JO, Olsen SN, Entova S, Oprian DD Biochemistry. 2017 Mar 15. doi: 10.1021/acs.biochem.7b00143. PMID:28272875[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Morehouse BR, Kumar RP, Matos JO, Olsen SN, Entova S, Oprian DD. Functional and Structural Characterization of a (+)-Limonene Synthase from Citrus sinensis. Biochemistry. 2017 Mar 15. doi: 10.1021/acs.biochem.7b00143. PMID:28272875 doi:http://dx.doi.org/10.1021/acs.biochem.7b00143
- ↑ Kumar RP, Morehouse BR, Matos JO, Malik K, Lin H, Krauss IJ, Oprian DD. Structural Characterization of Early Michaelis Complexes in the Reaction Catalyzed by (+)-Limonene Synthase from Citrus sinensis Using Fluorinated Substrate Analogues. Biochemistry. 2017 Mar 15. doi: 10.1021/acs.biochem.7b00144. PMID:28272876 doi:http://dx.doi.org/10.1021/acs.biochem.7b00144
- ↑ Morehouse BR, Kumar RP, Matos JO, Olsen SN, Entova S, Oprian DD. Functional and Structural Characterization of a (+)-Limonene Synthase from Citrus sinensis. Biochemistry. 2017 Mar 15. doi: 10.1021/acs.biochem.7b00143. PMID:28272875 doi:http://dx.doi.org/10.1021/acs.biochem.7b00143
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