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TitleSubstrate Trapping in Polyketide Synthase Thioesterase Domains: Structural Basis for Macrolactone Formation.
Journal, issue, pagesAcs Catalysis, Vol. 14, Page 12551-12563, Year 2024
Publish dateJun 19, 2024 (structure data deposition date)
AuthorsMcCullough, T.M. / Choudhary, V. / Akey, D.L. / Skiba, M.A. / Bernard, S.M. / Kittendorf, J.D. / Schmidt, J.J. / Sherman, D.H. / Smith, J.L.
External linksAcs Catalysis / PubMed:39927088
MethodsX-ray diffraction
Resolution1.44 - 3.1 Å
Structure data

PDB-9cbd:
Pikromycin Thioesterase Domain
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-9cel:
Juvenimicin Thioesterase
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

PDB-9cfj:
Fluvirucin Thioesterase Domain (FluC TE)
Method: X-RAY DIFFRACTION / Resolution: 1.44 Å

PDB-9cgl:
Pikromycin Thioesterase Doubly Protected DAP
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-9cgn:
Pikromycin Thioesterase with heptaketide adduct
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-9cgo:
Tylosin thioesterase domain (TylG5 TE)
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-GOL:
GLYCEROL

PDB-1awe:
HUMAN SOS1 PLECKSTRIN HOMOLOGY (PH) DOMAIN, NMR, 20 STRUCTURES

PDB-1awf:
NOVEL COVALENT THROMBIN INHIBITOR FROM PLANT EXTRACT

Source
  • streptomyces venezuelae (bacteria)
  • micromonospora chalcea subsp. izumensis (bacteria)
  • actinomadura vulgaris (bacteria)
  • streptomyces fradiae (bacteria)
KeywordsHYDROLASE / Polyketide synthase / PKS / Thioesterase / TE / Macrolactonization / Pikromycin / biosynthesis / natural products / thioesterase domain / TE Domain / PikAIV / Unnatural amino acid / UAA / DAP

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