The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation
| Autor: | Julian D. Hegemann, Olaf Burghaus, Andreas Mielcarek, Beata M. Wieckowski, Mohamed A. Marahiel, Linda Boss |
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| Jazyk: | angličtina |
| Předmět: |
Hydrolases
Operon Stereochemistry Ribosomal peptide Molecular Sequence Data Bacillus thuringiensis Biophysics Peptide Sulfides Biosynthesis Biochemistry Natural product Serine chemistry.chemical_compound [4Fe–4S] cluster Bacteriocins Thioether Structural Biology Genetics Amino Acid Sequence Asparagine Threonine Molecular Biology chemistry.chemical_classification Radical SAM enzyme Cell Biology chemistry Sactipeptide Radical SAM |
| Zdroj: | FEBS Letters. (15):1802-1806 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2015.05.032 |
| Popis: | Thurincin H is a 31-residue, ribosomally synthesized bacteriocin originating from the thn operon of Bacillus thuringiensis SF361. It is the only known sactipeptide carrying four thioether bridges between four cysteines and the α-carbons of a serine, an asparagine and two threonine residues. By analysis of the thn operon and use of in vitro studies we now reveal that ThnB is a radical S-adenosylmethionine (SAM) enzyme containing two [4Fe–4S] clusters. Furthermore, we confirm the involvement of ThnB in the formation of the thioether bonds present within the structure of thurincin H. Finally, we show that the PqqD homologous N-terminal domain of ThnB is essential for maturation of the thurincin H precursor peptide, but not for the SAM cleavage activity of ThnB. |
| Databáze: | OpenAIRE |
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