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The structure of CgnJ, a domain of unknown function protein from the crocagin gene cluster
- Source :
- Acta Crystallogr F Struct Biol Commun
- Publication Year :
- 2019
- Publisher :
- International Union of Crystallography (IUCr), 2019.
-
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 Ain 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 ofBacillus subtilis, ComJ, leading to the hypothesis of a similar role of the protein within the producing organism.
- Subjects :
- Protein Conformation
Biophysics
Regulator
Peptide
Computational biology
Bacillus subtilis
Crystallography, X-Ray
Peptides, Cyclic
Biochemistry
Research Communications
chemistry.chemical_compound
Biosynthesis
Structural Biology
Gene cluster
Genetics
chemistry.chemical_classification
Biological Products
biology
computer.file_format
Condensed Matter Physics
Protein Data Bank
biology.organism_classification
Enzyme
chemistry
Multigene Family
Protein Processing, Post-Translational
computer
Function (biology)
Protein Binding
Subjects
Details
- ISSN :
- 2053230X
- Volume :
- 75
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology Communications
- Accession number :
- edsair.doi.dedup.....4ee71fc4d54391056fa801fbbe471169
- Full Text :
- https://doi.org/10.1107/s2053230x19000712