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.firstpage731en_US
dc.citation.journalTitleThe Journal of Antibioticsen_US
dc.citation.lastpage740en_US
dc.citation.volumeNumber69en_US
dc.contributor.authorHuang, Tingtingen_US
dc.contributor.authorChang, Chin-Yuanen_US
dc.contributor.authorLohman, Jeremy R.en_US
dc.contributor.authorRudolf, Jeffrey D.en_US
dc.contributor.authorKim, Youngchangen_US
dc.contributor.authorChang, Changsooen_US
dc.contributor.authorYang, Dongen_US
dc.contributor.authorMa, Mingen_US
dc.contributor.authorYan, Xiaohuien_US
dc.contributor.authorCrnovcic, Ivanaen_US
dc.contributor.authorBigelow, Lanceen_US
dc.contributor.authorClancy, Shondaen_US
dc.contributor.authorBingman, Craig A.en_US
dc.contributor.authorYennamalli, Ragothaman M.en_US
dc.contributor.authorBabnigg, Gyorgyen_US
dc.contributor.authorJoachimiak, Andrzejen_US
dc.contributor.authorPhillips, George N.Jr.en_US
dc.contributor.authorShen, Benen_US
dc.date.accessioned2017-05-19T19:09:40Zen_US
dc.date.available2017-05-19T19:09:40Zen_US
dc.date.issued2016en_US
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.en_US
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.en_US
dc.identifier.doihttps://doi.org/10.1038/ja.2016.88en_US
dc.identifier.urihttps://hdl.handle.net/1911/94297en_US
dc.language.isoengen_US
dc.publisherSpringer Natureen_US
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer Nature.en_US
dc.titleCrystal structure of SgcJ, an NTF2-like superfamily protein involved in biosynthesis of the nine-membered enediyne antitumor antibiotic C-1027en_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpost-printen_US
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