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Structure paper

TitleInhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism.
Journal, issue, pagesJ. Biol. Chem., Vol. 276, Page 6551-6559, Year 2001
Publish dateAug 7, 2000 (structure data deposition date)
AuthorsPrice, A.C. / Choi, K.H. / Heath, R.J. / Li, Z. / White, S.W. / Rock, C.O.
External linksJ. Biol. Chem. / PubMed:11050088
MethodsX-ray diffraction
Resolution2.27 - 2.35 Å
Structure data

PDB-1fj4:
THE STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEX WITH THIOLACTOMYCIN, IMPLICATIONS FOR DRUG DESIGN
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-1fj8:
THE STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEX WITH CERULENIN, IMPLICATIONS FOR DRUG DESIGN
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

Chemicals

ChemComp-TLM:
THIOLACTOMYCIN

ChemComp-HOH:
WATER

ChemComp-CER:
(2S, 3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE / antifungal, antibiotic*YM

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / CONDENSING ENZYMES / FATTY ACID ELONGATION / THIOLACTOMYCIN / DRUG DESIGN / CERULENIN

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