The structure of CgnJ, a domain of unknown function protein from the crocagin gene cluster.
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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
SUBMITTER: Adam S
PROVIDER: S-EPMC6404859 | biostudies-literature | 2019 Mar
REPOSITORIES: biostudies-literature
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