2r0c
From Proteopedia
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| - | + | {{STRUCTURE_2r0c| PDB=2r0c | SCENE= }} | |
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'''Structure of the substrate-free form of the rebeccamycin biosynthetic enzyme REBC''' | '''Structure of the substrate-free form of the rebeccamycin biosynthetic enzyme REBC''' | ||
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[[Category: Drennan, C L.]] | [[Category: Drennan, C L.]] | ||
[[Category: Ryan, K S.]] | [[Category: Ryan, K S.]] | ||
| - | [[Category: | + | [[Category: Flavin adenine dinucleotide]] |
| - | [[Category: | + | [[Category: Monooxygenase]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:01:01 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:01, 4 May 2008
Structure of the substrate-free form of the rebeccamycin biosynthetic enzyme 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
2R0C is a Single protein structure of sequence from Lechevalieria aerocolonigenes. 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 Sun May 4 16:01:01 2008
