Details
| Original language | English |
|---|---|
| Pages (from-to) | 205-211 |
| Number of pages | 7 |
| Journal | Acta Crystallographica Section F: Structural Biology Communications |
| Volume | 75 |
| Publication status | Published - 2019 |
| Externally published | Yes |
Abstract
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.
Keywords
- CgnJ, crocagin, domains of unknown function, RiPPs
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Physics and Astronomy(all)
- Condensed Matter Physics
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In: Acta Crystallographica Section F: Structural Biology Communications, Vol. 75, 2019, p. 205-211.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The structure of CgnJ, a domain of unknown function protein from the crocagin gene cluster
AU - Adam, Sebastian
AU - Klein, Andreas
AU - Surup, Frank
AU - Koehnke, Jesko
PY - 2019
Y1 - 2019
N2 - 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.
AB - 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.
KW - CgnJ
KW - crocagin
KW - domains of unknown function
KW - RiPPs
UR - http://www.scopus.com/inward/record.url?scp=85062611248&partnerID=8YFLogxK
U2 - 10.1107/S2053230X19000712
DO - 10.1107/S2053230X19000712
M3 - Article
C2 - 30839296
AN - SCOPUS:85062611248
VL - 75
SP - 205
EP - 211
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
SN - 2053-230X
ER -