Structure of limonene synthase, a simple model for terpenoid cyclase catalysis.
The crystal structure of (4S)-limonene synthase from Mentha spic ata, a metal ion-dependent monoterpene cyclase that catalyzes the coupled isomerization and cyclization of geranyl diphosphate, is reported at 2.7-A; resolution in two forms liganded to the substrate and intermediate analogs, 2-fluorogeranyl diphosphate and 2-fluorolinalyl diphosphate, respectively. The implications of these findings are described for domain interactions in the homodimer and for changes in diphosphate-metal ion coordination and substrate binding conformation in the course of the multistep reaction.
Hyatt
David C
DC
Institute of Biological Chemistry, Washingston State University, Pullman, WA 99164-6340, USA.
Youn
Buhyun
B
Zhao
Yuxin
Y
Santhamma
Bindu
B
Coates
Robert M
RM
Croteau
Rodney B
RB
Kang
ChulHee
C
D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D019753:Intramolecular Lyases / Q000737:chemistry* / Q000378:metabolism; D007477:Ions; D008024:Ligands; D031337:Mentha spicata / Q000201:enzymology; D008956:Models, Chemical; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D013729:Terpenes / Q000737:chemistry*
D007477:Ions; D008024:Ligands; D010940:Plant Proteins; D013729:Terpenes; D019753:Intramolecular Lyases; C040265:pinene cyclase I