2r0p: Difference between revisions

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==Overview==

The biosynthesis of rebeccamycin, an antitumor compound, involves the, remarkable eight-electron oxidation of chlorinated chromopyrrolic acid., Although one rebeccamycin biosynthetic enzyme is capable of generating low, levels of the eight-electron oxidation product on its own, a second, protein, RebC, is required to accelerate product formation and eliminate, side reactions. However, the mode of action of RebC was largely unknown., Using crystallography, we have determined a likely function for RebC as a, flavin hydroxylase, captured two snapshots of its dynamic catalytic cycle, and trapped a reactive molecule, a putative substrate, in its binding, pocket. These studies strongly suggest that the role of RebC is to, sequester a reactive intermediate produced by its partner protein and to, react with it enzymatically, preventing its conversion to a suite of, degradation products that includes, at low levels, the desired product.

The biosynthesis of rebeccamycin, an antitumor compound, involves the remarkable eight-electron oxidation of chlorinated chromopyrrolic acid. Although one rebeccamycin biosynthetic enzyme is capable of generating low levels of the eight-electron oxidation product on its own, a second protein, RebC, is required to accelerate product formation and eliminate side reactions. However, the mode of action of RebC was largely unknown. Using crystallography, we have determined a likely function for RebC as a flavin hydroxylase, captured two snapshots of its dynamic catalytic cycle, and trapped a reactive molecule, a putative substrate, in its binding pocket. These studies strongly suggest that the role of RebC is to sequester a reactive intermediate produced by its partner protein and to react with it enzymatically, preventing its conversion to a suite of degradation products that includes, at low levels, the desired product.

==About this Structure==

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==Reference==

Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC., Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL, Proc Natl Acad Sci U S A. 2007 Sep 14;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17873060 17873060]

Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC., Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL, Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15311-6. Epub 2007 Sep 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17873060 17873060]

[[Category: Lechevalieria aerocolonigenes]]

[[Category: Single protein]]

[[Category: Drennan, C.L.]]

[[Category: Drennan, C L.]]

[[Category: Ryan, K.S.]]

[[Category: Ryan, K S.]]

[[Category: CL]]

[[Category: FAD]]

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[[Category: oxidoreductase]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The biosynthesis of rebeccamycin, an antitumor compound, involves the, remarkable eight-electron oxidation of chlorinated chromopyrrolic acid., Although one rebeccamycin biosynthetic enzyme is capable of generating low, levels of the eight-electron oxidation product on its own, a second, protein, RebC, is required to accelerate product formation and eliminate, side reactions. However, the mode of action of RebC was largely unknown., Using crystallography, we have determined a likely function for RebC as a, flavin hydroxylase, captured two snapshots of its dynamic catalytic cycle, and trapped a reactive molecule, a putative substrate, in its binding, pocket. These studies strongly suggest that the role of RebC is to, sequester a reactive intermediate produced by its partner protein and to, react with it enzymatically, preventing its conversion to a suite of, degradation products that includes, at low levels, the desired product.
+The biosynthesis of rebeccamycin, an antitumor compound, involves the remarkable eight-electron oxidation of chlorinated chromopyrrolic acid. Although one rebeccamycin biosynthetic enzyme is capable of generating low levels of the eight-electron oxidation product on its own, a second protein, RebC, is required to accelerate product formation and eliminate side reactions. However, the mode of action of RebC was largely unknown. Using crystallography, we have determined a likely function for RebC as a flavin hydroxylase, captured two snapshots of its dynamic catalytic cycle, and trapped a reactive molecule, a putative substrate, in its binding pocket. These studies strongly suggest that the role of RebC is to sequester a reactive intermediate produced by its partner protein and to react with it enzymatically, preventing its conversion to a suite of degradation products that includes, at low levels, the desired product.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC., Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL, Proc Natl Acad Sci U S A. 2007 Sep 14;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17873060 17873060]
+Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC., Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL, Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15311-6. Epub 2007 Sep 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17873060 17873060]
 [[Category: Lechevalieria aerocolonigenes]]
 [[Category: Single protein]]
-[[Category: Drennan, C.L.]]
+[[Category: Drennan, C L.]]
-[[Category: Ryan, K.S.]]
+[[Category: Ryan, K S.]]
 [[Category: CL]]
 [[Category: FAD]]
@@ Line 23: / Line 23: @@
 [[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:30:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:49 2008''