2r0c | pdb_00002r0c
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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 with CL and FAD 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 14;. PMID:17873060
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