ArticleThe Journal of antibiotics2016
Crystal structure of SgcJ, an NTF2-like superfamily protein involved in biosynthesis of the nine-membered enediyne antitumor antibiotic C-1027.
Article in The Journal of antibiotics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Article
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- Conformational spread drives the evolution of the calcium-calmodulin protein kinase II.Scientific reports · 2022Article
- Mcc1229, an Stx2a-Amplifying Microcin, Is ProducedInfection and immunity · 2022Article
- Structure and Function of a Dual Reductase-Dehydratase Enzyme System Involved inACS chemical biology · 2021Article
- Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Structural characterization of three noncanonical NTF2-like superfamily proteins: implications for polyketide biosynthesis.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Comparative transcriptomic analysis reveals the significant pleiotropic regulatory effects of LmbU on lincomycin biosynthesis.Microbial cell factories · 2020Article
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Authors and funding
18 authors at 5 institutions in 1 country.
Funding
Abstract
Comparative analysis of the enediyne biosynthetic gene clusters revealed sets of conserved genes serving as outstanding candidates for the enediyne core. Here we report the crystal structures of SgcJ and its homologue NCS-Orf16, together with gene inactivation and site-directed mutagenesis studies, to gain insight into enediyne core biosynthesis. Gene inactivation in vivo establishes that SgcJ is required for C-1027 production in Streptomyces globisporus. SgcJ and NCS-Orf16 share a common structure with the nuclear transport factor 2-like superfamily of proteins, featuring a putative substrate binding or catalytic active site. Site-directed mutagenesis of the conserved residues lining this site allowed us to propose that SgcJ and its homologues may play a catalytic role in transforming the linear polyene intermediate, along with other enediyne polyketide synthase-associated enzymes, into an enzyme-sequestered enediyne core intermediate. These findings will help formulate hypotheses and design experiments to ascertain the function of SgcJ and its homologues in nine-membered enediyne core biosynthesis.
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