2r0p
From Proteopedia
(New page: 200px<br /><applet load="2r0p" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r0p, resolution 2.1Å" /> '''K252c-soaked RebC'''<...) |
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==Overview== | ==Overview== | ||
| - | The biosynthesis of rebeccamycin, an antitumor compound, involves the | + | 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== | ==About this Structure== | ||
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==Reference== | ==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 | + | 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: Lechevalieria aerocolonigenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Drennan, C | + | [[Category: Drennan, C L.]] |
| - | [[Category: Ryan, K | + | [[Category: Ryan, K S.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:49 2008'' |
Revision as of 16:43, 21 February 2008
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K252c-soaked RebC
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.
About this Structure
2R0P is a Single protein structure of sequence from Lechevalieria aerocolonigenes with , and as ligands. Full crystallographic information is available from OCA.
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 25;104(39):15311-6. Epub 2007 Sep 14. PMID:17873060
Page seeded by OCA on Thu Feb 21 18:43:49 2008
