Structure Prediction and Genome Mining‐Aided Discovery of the Bacterial C‐Terminal Tryptophan Prenyltransferase PalQ
Abstract Post‐translational prenylations, found in eukaryotic primary metabolites and bacterial secondary metabolites, play crucial roles in biomolecular interactions. Employing genome mining methods combined with AlphaFold2‐based predictions of protein interactions, PalQ , a prenyltransferase respo...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Wiley
2024-02-01
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| Series: | Advanced Science |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/advs.202307372 |
| _version_ | 1797319210608623616 |
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| author | Azusa Miyata Sohei Ito Daisuke Fujinami |
| author_facet | Azusa Miyata Sohei Ito Daisuke Fujinami |
| author_sort | Azusa Miyata |
| collection | DOAJ |
| description | Abstract Post‐translational prenylations, found in eukaryotic primary metabolites and bacterial secondary metabolites, play crucial roles in biomolecular interactions. Employing genome mining methods combined with AlphaFold2‐based predictions of protein interactions, PalQ , a prenyltransferase responsible for the tryptophan prenylation of RiPPs produced by Paenibacillus alvei, is identified. PalQ differs from cyanobactin prenyltransferases because of its evolutionary relationship to isoprene synthases, which enables PalQ to transfer extended prenyl chains to the indole C3 position. This prenylation introduces structural diversity to the tryptophan side chain and also leads to conformational dynamics in the peptide backbone, attributed to the cis/trans isomerization that arises from the formation of a pyrrolidine ring. Additionally, PalQ exhibited pronounced positional selectivity for the C‐terminal tryptophan. Such enzymatic characteristics offer a toolkit for peptide therapeutic lipidation. |
| first_indexed | 2024-03-08T04:03:33Z |
| format | Article |
| id | doaj.art-5b9cc45e381b4b2e9f846e52cf80e5ec |
| institution | Directory Open Access Journal |
| issn | 2198-3844 |
| language | English |
| last_indexed | 2024-03-08T04:03:33Z |
| publishDate | 2024-02-01 |
| publisher | Wiley |
| record_format | Article |
| series | Advanced Science |
| spelling | doaj.art-5b9cc45e381b4b2e9f846e52cf80e5ec2024-02-09T08:26:35ZengWileyAdvanced Science2198-38442024-02-01116n/an/a10.1002/advs.202307372Structure Prediction and Genome Mining‐Aided Discovery of the Bacterial C‐Terminal Tryptophan Prenyltransferase PalQAzusa Miyata0Sohei Ito1Daisuke Fujinami2Graduate Division of Nutritional and Environmental Sciences University of Shizuoka 52‐1 Yada, Suruga‐ku Shizuoka 422‐8526 JapanGraduate Division of Nutritional and Environmental Sciences University of Shizuoka 52‐1 Yada, Suruga‐ku Shizuoka 422‐8526 JapanGraduate Division of Nutritional and Environmental Sciences University of Shizuoka 52‐1 Yada, Suruga‐ku Shizuoka 422‐8526 JapanAbstract Post‐translational prenylations, found in eukaryotic primary metabolites and bacterial secondary metabolites, play crucial roles in biomolecular interactions. Employing genome mining methods combined with AlphaFold2‐based predictions of protein interactions, PalQ , a prenyltransferase responsible for the tryptophan prenylation of RiPPs produced by Paenibacillus alvei, is identified. PalQ differs from cyanobactin prenyltransferases because of its evolutionary relationship to isoprene synthases, which enables PalQ to transfer extended prenyl chains to the indole C3 position. This prenylation introduces structural diversity to the tryptophan side chain and also leads to conformational dynamics in the peptide backbone, attributed to the cis/trans isomerization that arises from the formation of a pyrrolidine ring. Additionally, PalQ exhibited pronounced positional selectivity for the C‐terminal tryptophan. Such enzymatic characteristics offer a toolkit for peptide therapeutic lipidation.https://doi.org/10.1002/advs.202307372genome miningpost‐translational modificationprenylationstructure prediction |
| spellingShingle | Azusa Miyata Sohei Ito Daisuke Fujinami Structure Prediction and Genome Mining‐Aided Discovery of the Bacterial C‐Terminal Tryptophan Prenyltransferase PalQ Advanced Science genome mining post‐translational modification prenylation structure prediction |
| title | Structure Prediction and Genome Mining‐Aided Discovery of the Bacterial C‐Terminal Tryptophan Prenyltransferase PalQ |
| title_full | Structure Prediction and Genome Mining‐Aided Discovery of the Bacterial C‐Terminal Tryptophan Prenyltransferase PalQ |
| title_fullStr | Structure Prediction and Genome Mining‐Aided Discovery of the Bacterial C‐Terminal Tryptophan Prenyltransferase PalQ |
| title_full_unstemmed | Structure Prediction and Genome Mining‐Aided Discovery of the Bacterial C‐Terminal Tryptophan Prenyltransferase PalQ |
| title_short | Structure Prediction and Genome Mining‐Aided Discovery of the Bacterial C‐Terminal Tryptophan Prenyltransferase PalQ |
| title_sort | structure prediction and genome mining aided discovery of the bacterial c terminal tryptophan prenyltransferase palq |
| topic | genome mining post‐translational modification prenylation structure prediction |
| url | https://doi.org/10.1002/advs.202307372 |
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