2r0p
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(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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Revision as of 11:30, 23 January 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 14;. PMID:17873060
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