Structure and Biosynthesis of Crocagins: Polycyclic Posttranslationally Modified Ribosomal Peptides from <i>Chondromyces crocatus</i>

Viehrig, Konrad; Surup, Frank; Volz, Carsten; Herrmann, Jennifer; Fayad, Antoine Abou; Adam, Sebastian; Köhnke, Jesko; Trauner, Dirk; Müller, Rolf

doi:10.1002/anie.201612640

Cited by 37 publications

(52 citation statements)

References 27 publications

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“…[1] Av ery recent addition to this fascinating class is crocagin A( 1), which was isolated by Müller et al from the myxobacterium Chondromyces crocatus, ap rolific producer of biologically active metabolites. [2] Crocagin Ai su nusual in several respects (Scheme 1). Biosynthetically,i ts tems from the Cterminus of ap recursor peptide (CgnA, 2), which undergoes cleavage,oxidation, and cyclization to yield the novel heterotricyclic system of 1.…”

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Total Synthesis of Crocagin A

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Crocagin A (1) combines an attractive molecular structure with an unusual biosynthesis and bioactivity. An efficient synthesis of crocagin A is presented that hinges on an early formation of the heterotricyclic core, an electrophilic amination, and the stereoselective hydrogenation of a tetrasubstituted double bond. This synthesis confirms the absolute configuration of crocagin A and provides access to the natural product and derivatives thereof for further biological testing.

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Total Synthesis of Crocagin A

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“…The use of these techniques led to the recent identification and isolation of the crocagins, a novel group of polycyclic RiPPs from Chondromyces crocatus Cm c5 containing a tetrahydropyrrolo-[2,3-b]-indole core ( Fig. 1a) (Viehrig et al, 2017). While searching for potential activities of these natural products, they were discovered to bind carbon-storage regulator A (CsrA; Viehrig et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

“…1a) (Viehrig et al, 2017). While searching for potential activities of these natural products, they were discovered to bind carbon-storage regulator A (CsrA; Viehrig et al, 2017). CsrA is a highly conserved key player in the Csr-type regulatory system, an important post-transcriptional control mechanism involving small regulatory RNAs (sRNAs), which coordinates the expression of a variety of proteins, including specific virulence factors, as well as biofilm formation (Maurer et al, 2016).…”

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confidence: 99%

“…In addition to the natural products, the biosynthetic gene cluster of crocagins was identified by a combination of genome analysis, targeted gene inactivation of the producer and in vitro experiments (Fig. 1b;Viehrig et al, 2017). Within the gene cluster, nine potentially biosynthetic genes (cgnB-cgnE, cgnI-cgnL and cgnMT) have been identified and putative functions have been assigned by sequence homology (Viehrig et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

“…1b;Viehrig et al, 2017). Within the gene cluster, nine potentially biosynthetic genes (cgnB-cgnE, cgnI-cgnL and cgnMT) have been identified and putative functions have been assigned by sequence homology (Viehrig et al, 2017). cgnA encodes the precursor peptide containing the core peptide sequence IYW ( Fig.…”

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confidence: 99%

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The structure of CgnJ, a domain of unknown function protein from the crocagin gene cluster

et al. 2019

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Natural products often contain interesting new chemical entities that are introduced into the structure of a compound by the enzymatic machinery of the producing organism. The recently described crocagins are novel polycyclic peptides which belong to the class of ribosomally synthesized and post‐translationally modified peptide natural products. They have been shown to bind to the conserved prokaryotic carbon‐storage regulator A in vitro. In efforts to understand crocagin biosynthesis, the putative biosynthetic genes were expressed and purified. Here, the first crystal structure of a protein from the crocagin‐biosynthetic gene cluster, CgnJ, a domain of unknown function protein, is reported. Possible functions of this protein were explored by structural and sequence homology analyses. Even though the sequence homology to proteins in the Protein Data Bank is low, the protein shows significant structural homology to a protein with known function within the competency system of Bacillus subtilis, ComJ, leading to the hypothesis of a similar role of the protein within the producing organism.

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Total Synthesis of Crocagin A

Bihelovic¹,

Stichnoth²,

Müller³

et al. 2017

Angewandte Chemie

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Crocagin A( 1)c ombines an attractive molecular structure with an unusual biosynthesis and bioactivity.A n efficient synthesis of crocagin Aispresented that hinges on an early formation of the heterotricyclic core,a ne lectrophilic amination, and the stereoselective hydrogenation of atetrasubstituted double bond. This synthesis confirms the absolute configuration of crocagin Aand provides access to the natural product and derivatives thereof for further biological testing. Scheme 1. Structure and biosynthetic origin of crocagin.Scheme 2. Retrosynthetic analysis of crocagin A.

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Structure and Biosynthesis of Crocagins: Polycyclic Posttranslationally Modified Ribosomal Peptides from Chondromyces crocatus

Cited by 37 publications

References 27 publications

Total Synthesis of Crocagin A

Total Synthesis of Crocagin A

The structure of CgnJ, a domain of unknown function protein from the crocagin gene cluster

Total Synthesis of Crocagin A

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