2R0P
K252c-soaked RebC
Summary for 2R0P
| Entry DOI | 10.2210/pdb2r0p/pdb |
| Related | 2R0C 2R0G |
| Descriptor | RebC, CHLORIDE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | flavin adenine dinucleotide, k252c, monooxygenase, oxidoreductase |
| Biological source | Lechevalieria aerocolonigenes |
| Total number of polymer chains | 1 |
| Total formula weight | 61059.97 |
| Authors | Ryan, K.S.,Drennan, C.L. (deposition date: 2007-08-20, release date: 2007-09-25, Last modification date: 2023-08-30) |
| Primary citation | Ryan, K.S.,Howard-Jones, A.R.,Hamill, M.J.,Elliott, S.J.,Walsh, C.T.,Drennan, C.L. Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC Proc.Natl.Acad.Sci.Usa, 104:15311-15316, 2007 Cited by PubMed Abstract: 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. PubMed: 17873060DOI: 10.1073/pnas.0707190104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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