7ABB
The truncated structure of the Bottromycin biosynthetic protein SalCYP
Summary for 7ABB
| Entry DOI | 10.2210/pdb7abb/pdb |
| Descriptor | SalCYP truncation, HEME C (3 entities in total) |
| Functional Keywords | biosynthetic protein, cytochrome, p450, bottromycin |
| Biological source | Salinispora tropica |
| Total number of polymer chains | 1 |
| Total formula weight | 44399.16 |
| Authors | Adam, S.,Koehnke, J. (deposition date: 2020-09-07, release date: 2020-12-02, Last modification date: 2024-01-31) |
| Primary citation | Adam, S.,Franz, L.,Milhim, M.,Bernhardt, R.,Kalinina, O.V.,Koehnke, J. Characterization of the Stereoselective P450 Enzyme BotCYP Enables the In Vitro Biosynthesis of the Bottromycin Core Scaffold. J.Am.Chem.Soc., 142:20560-20565, 2020 Cited by PubMed Abstract: Bottromycins are ribosomally synthesized and post-translationally modified peptide natural product antibiotics that are effective against high-priority human pathogens such as methicillin-resistant . The total synthesis of bottromycins involves at least 17 steps, with a poor overall yield. Here, we report the characterization of the cytochrome P450 enzyme BotCYP from a bottromycin biosynthetic gene cluster. We determined the structure of a close BotCYP homolog and used our data to conduct the first large-scale survey of P450 enzymes associated with RiPP biosynthetic gene clusters. We demonstrate that BotCYP converts a C-terminal thiazoline to a thiazole via an oxidative decarboxylation reaction and provides stereochemical resolution for the pathway. Our data enable the two-pot production of the bottromycin core scaffold and may allow the rapid generation of bottromycin analogues for compound development. PubMed: 33249843DOI: 10.1021/jacs.0c10361 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.50004339457 Å) |
Structure validation
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