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TitleFunctional and structural studies on the esperamicin thioesterase and progress toward understanding enediyne core biosynthesis
Journal, issue, pagesTo Be Published
Publish dateJun 23, 2024 (structure data deposition date)
AuthorsHankore, E.D. / Miller, M.D. / Kosgei, A.J. / Xu, W. / Tan, K. / Endres, M. / Bhardwaj, M. / Joachimiak, G. / Joachimiak, A. / Phillips Jr., G.N. ...Hankore, E.D. / Miller, M.D. / Kosgei, A.J. / Xu, W. / Tan, K. / Endres, M. / Bhardwaj, M. / Joachimiak, G. / Joachimiak, A. / Phillips Jr., G.N. / Thorson, J.S. / Van Lanen, S.G.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.57 Å
Structure data

PDB-9ccr:
Crystal structure of the EspE7 thioesterase mutant R35A from the esperamicin biosynthetic pathway at 1.6 A
Method: X-RAY DIFFRACTION / Resolution: 1.57 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-DCC:
DODECYL-COA

ChemComp-HOH:
WATER

Source
  • actinomadura verrucosospora (bacteria)
KeywordsHYDROLASE / thioesterase / hot-dog / enediyne biosynthetic pathway / esperamicin biosynthesis / Natural product biosynthesis

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