Crystal structure of SgcJ, an NTF2-like superfamily protein involved in biosynthesis of the nine-membered enediyne antitumor antibiotic C-1027

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dc.citation.firstpage731
dc.citation.journalTitleThe Journal of Antibiotics
dc.citation.lastpage740
dc.citation.volumeNumber69
dc.contributor.authorHuang, Tingting
dc.contributor.authorChang, Chin-Yuan
dc.contributor.authorLohman, Jeremy R.
dc.contributor.authorRudolf, Jeffrey D.
dc.contributor.authorKim, Youngchang
dc.contributor.authorChang, Changsoo
dc.contributor.authorYang, Dong
dc.contributor.authorMa, Ming
dc.contributor.authorYan, Xiaohui
dc.contributor.authorCrnovcic, Ivana
dc.contributor.authorBigelow, Lance
dc.contributor.authorClancy, Shonda
dc.contributor.authorBingman, Craig A.
dc.contributor.authorYennamalli, Ragothaman M.
dc.contributor.authorBabnigg, Gyorgy
dc.contributor.authorJoachimiak, Andrzej
dc.contributor.authorPhillips, George N.Jr.
dc.contributor.authorShen, Ben
dc.date.accessioned2017-05-19T19:09:40Z
dc.date.available2017-05-19T19:09:40Z
dc.date.issued2016
dc.description.abstractComparative 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.
dc.identifier.citationHuang, Tingting, Chang, Chin-Yuan, Lohman, Jeremy R., et al.. "Crystal structure of SgcJ, an NTF2-like superfamily protein involved in biosynthesis of the nine-membered enediyne antitumor antibiotic C-1027." <i>The Journal of Antibiotics,</i> 69, (2016) Springer Nature: 731-740. https://doi.org/10.1038/ja.2016.88.
dc.identifier.doihttps://doi.org/10.1038/ja.2016.88
dc.identifier.urihttps://hdl.handle.net/1911/94297
dc.language.isoeng
dc.publisherSpringer Nature
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer Nature.
dc.titleCrystal structure of SgcJ, an NTF2-like superfamily protein involved in biosynthesis of the nine-membered enediyne antitumor antibiotic C-1027
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpost-print
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