4OVM

Crystal structure of SgcJ protein from Streptomyces carzinostaticus

Summary for 4OVM

• Entry DOI: 10.2210/pdb4ovm/pdb
• Related: 4I4K
• Descriptor: uncharacterized protein SgcJ (2 entities in total)
• Functional Keywords: neocarzinostatin biosynthesis, unknown funciton, psi-biology, midwest center for structural genomics, mcsg, enzyme discovery for natural product biosynthesis, natpro, structural genomics, unknown function
• Biological source: Streptomyces carzinostaticus subsp. neocarzinostaticus
• Total number of polymer chains: 10
• Total formula weight: 156307.15

Authors

Chang, C.,Bigelow, L.,Clancy, S.,Bingman, C.A.,Yennamalli, R.,Lohman, J.R.,Ma, M.,Shen, B.,Phillips Jr., G.N.,Babnigg, G.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG),Enzyme Discovery for Natural Product Biosynthesis (NatPro) (deposition date: 2013-11-20, release date: 2013-12-25, Last modification date: 2024-11-06)

Primary citation

Huang, T.,Chang, C.Y.,Lohman, J.R.,Rudolf, J.D.,Kim, Y.,Chang, C.,Yang, D.,Ma, M.,Yan, X.,Crnovcic, I.,Bigelow, L.,Clancy, S.,Bingman, C.A.,Yennamalli, R.M.,Babnigg, G.,Joachimiak, A.,Phillips, G.N.,Shen, B.
Crystal structure of SgcJ, an NTF2-like superfamily protein involved in biosynthesis of the nine-membered enediyne antitumor antibiotic C-1027.
J.Antibiot., 2016

PubMed 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.

PubMed: 27406907
DOI: 10.1038/ja.2016.88

Experimental method

X-RAY DIFFRACTION (2.719 Å)