ArticleIUCrJ2019
Crystal structure of the putative cyclase IdmH from the indanomycin nonribosomal peptide synthase/polyketide synthase.
Article in IUCrJ, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Iminium Catalysis in Natural Diels-Alderase.Nature catalysis · 2025Article
- Pattern-Based Genome Mining Guides Discovery of the Antibiotic Indanopyrrole A from a Marine Streptomycete.Journal of natural products · 2024Article
- Pattern-based genome mining guides discovery of the antibiotic indanopyrrole A from a marine streptomycetef.bioRxiv : the preprint server for biology · 2024Article
- Article
- Iron-sulphur protein catalysed [4+2] cycloadditions in natural product biosynthesis.Nature communications · 2024Article
- Boosting the Full Potential of PyMOL with Structural Biology Plugins.Biomolecules · 2022Review
- A particle size threshold governs diffusion and segregation of PAR-3 during cell polarization.Cell reports · 2022Article
- Discovery and investigation of natural Diels-Alderases.Journal of natural medicines · 2021Review
- Catalytic mechanism andNature catalysis · 2021Article
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Authors and funding
7 authors.
Funding
Abstract
Indanomycin is biosynthesized by a hybrid nonribosomal peptide synthase/polyketide synthase (NRPS/PKS) followed by a number of 'tailoring' steps to form the two ring systems that are present in the mature product. It had previously been hypothesized that the indane ring of indanomycin was formed by the action of IdmH using a Diels-Alder reaction. Here, the crystal structure of a selenomethionine-labelled truncated form of IdmH (IdmH-Δ99-107) was solved using single-wavelength anomalous dispersion (SAD) phasing. This truncated variant allows consistent and easy crystallization, but importantly the structure was used as a search model in molecular replacement, allowing the full-length IdmH structure to be determined to 2.7 Å resolution. IdmH is a homodimer, with the individual protomers consisting of an α+β barrel. Each protomer contains a deep hydrophobic pocket which is proposed to constitute the active site of the enzyme. To investigate the reaction catalysed by IdmH, 88% of the backbone NMR resonances were assigned, and using chemical shift perturbation of [
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