2ong: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: Single protein]]

[[Category: Croteau, R.]]

[[Category: Hyatt, D.C.]]

[[Category: Hyatt, D C.]]

[[Category: Kang, C.]]

[[Category: Youn, B.]]

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[[Category: monoterpene synthase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:26 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Croteau, R.]]
-[[Category: Hyatt, D.C.]]
+[[Category: Hyatt, D C.]]
 [[Category: Kang, C.]]
 [[Category: Youn, B.]]
@@ Line 28: / Line 28: @@
 [[Category: monoterpene synthase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:32:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:26 2008''