6I5S
AH, Bottromycin amidohydrolase
Summary for 6I5S
| Entry DOI | 10.2210/pdb6i5s/pdb |
| Descriptor | bottromycin amidohydrolase, ZINC ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | gatekeeper enzyme, bottromycin, amidohydrolase, hydrolase |
| Biological source | Streptomyces purpureus |
| Total number of polymer chains | 1 |
| Total formula weight | 51248.90 |
| Authors | Koehnke, J.,Sikandar, A. (deposition date: 2018-11-14, release date: 2019-09-25, Last modification date: 2025-04-09) |
| Primary citation | Sikandar, A.,Franz, L.,Melse, O.,Antes, I.,Koehnke, J. Thiazoline-Specific Amidohydrolase PurAH Is the Gatekeeper of Bottromycin Biosynthesis. J.Am.Chem.Soc., 141:9748-9752, 2019 Cited by PubMed Abstract: The ribosomally synthesized and post-translationally modified peptide (RiPP) bottromycin A2 possesses potent antimicrobial activity. Its biosynthesis involves the enzymatic formation of a macroamidine, a process previously suggested to require the concerted efforts of a YcaO enzyme (PurCD) and an amidohydrolase (PurAH) in vivo. In vitro, PurCD alone is sufficient to catalyze formation of the macroamidine, but the process is reversible. We set out to probe the role of PurAH in macroamidine formation in vitro. We demonstrate that PurAH is highly selective for macroamidine-containing precursor peptides and cleaves C-terminal of a thiazoline, thus removing the follower peptide. After follower cleavage, macroamidine formation is irreversible, indicating PurAH as the gatekeeper of bottromycin biosynthesis. The structure of PurAH suggests residues involved in catalysis, which were probed through mutagenesis. PubMed: 31192589DOI: 10.1021/jacs.8b12231 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.73 Å) |
Structure validation
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