2d52: Difference between revisions

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==Overview==

The crystal structures of a wild-type and a mutant PCS, a novel plant type, III polyketide synthase from a medicinal plant, Aloe arborescens, were, solved at 1.6 A resolution. The crystal structures revealed that the, pentaketide-producing wild-type and the octaketide-producing M207G mutant, shared almost the same overall folding, and that the large-to-small, substitution dramatically increases the volume of the, polyketide-elongation tunnel by opening a gate to two hidden pockets, behind the active site of the enzyme. The chemically inert active site, residue 207 thus controls the number of condensations of malonyl-CoA, solely depending on the steric bulk of the side chain. These findings not, only provided insight into the polyketide formation reaction, but they, also suggested strategies for the engineered biosynthesis of polyketides.

The crystal structures of a wild-type and a mutant PCS, a novel plant type III polyketide synthase from a medicinal plant, Aloe arborescens, were solved at 1.6 A resolution. The crystal structures revealed that the pentaketide-producing wild-type and the octaketide-producing M207G mutant shared almost the same overall folding, and that the large-to-small substitution dramatically increases the volume of the polyketide-elongation tunnel by opening a gate to two hidden pockets behind the active site of the enzyme. The chemically inert active site residue 207 thus controls the number of condensations of malonyl-CoA, solely depending on the steric bulk of the side chain. These findings not only provided insight into the polyketide formation reaction, but they also suggested strategies for the engineered biosynthesis of polyketides.

==About this Structure==

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[[Category: polyketide synthase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:25 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structures of a wild-type and a mutant PCS, a novel plant type, III polyketide synthase from a medicinal plant, Aloe arborescens, were, solved at 1.6 A resolution. The crystal structures revealed that the, pentaketide-producing wild-type and the octaketide-producing M207G mutant, shared almost the same overall folding, and that the large-to-small, substitution dramatically increases the volume of the, polyketide-elongation tunnel by opening a gate to two hidden pockets, behind the active site of the enzyme. The chemically inert active site, residue 207 thus controls the number of condensations of malonyl-CoA, solely depending on the steric bulk of the side chain. These findings not, only provided insight into the polyketide formation reaction, but they, also suggested strategies for the engineered biosynthesis of polyketides.
+The crystal structures of a wild-type and a mutant PCS, a novel plant type III polyketide synthase from a medicinal plant, Aloe arborescens, were solved at 1.6 A resolution. The crystal structures revealed that the pentaketide-producing wild-type and the octaketide-producing M207G mutant shared almost the same overall folding, and that the large-to-small substitution dramatically increases the volume of the polyketide-elongation tunnel by opening a gate to two hidden pockets behind the active site of the enzyme. The chemically inert active site residue 207 thus controls the number of condensations of malonyl-CoA, solely depending on the steric bulk of the side chain. These findings not only provided insight into the polyketide formation reaction, but they also suggested strategies for the engineered biosynthesis of polyketides.
 ==About this Structure==
@@ Line 20: / Line 20: @@
 [[Category: polyketide synthase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:14:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:25 2008''