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TitleThe structural organization of trans-AT polyketide synthases: ketoacyl synthase and trans-acting enoyl reductase
Journal, issue, pagesTo Be Published
Publish dateMar 31, 2015 (structure data deposition date)
AuthorsMartin, S.F. / Jakob, R.P. / Herbst, D.A. / Maier, T.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.998 - 2.8 Å
Structure data

PDB-4z37:
Structure of the ketosynthase of module 2 of C0ZGQ5 (trans-AT PKS) from Brevibacillus brevis
Method: X-RAY DIFFRACTION / Resolution: 1.998 Å

PDB-4z38:
Crystal structure of enoyl reductase domain of MlnA from the macrolactin biosynthesis cluster from Bacillus amyloliquefaciens
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

Source
  • brevibacillus brevis (strain 47 / jcm 6285 / nbrc 100599) (bacteria)
  • bacillus amyloliquefaciens subsp. plantarum (strain dsm 23117 / bgsc 10a6 / fzb42) (bacteria)
KeywordsTRANSFERASE / polyketide / ketosynthase / trans-AT / AT-less / pks / enoyl reductase / trans-AT PKS / TIM barrel

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