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Structure paper

TitleInduced-Fit Upon Ligand Binding Revealed by Crystal Structures of the Hot-Dog Fold Thioesterase in Dynemicin Biosynthesis.
Journal, issue, pagesJ. Mol. Biol., Vol. 404, Page 291-, Year 2010
Publish dateMay 17, 2010 (structure data deposition date)
AuthorsLiew, C.W. / Sharff, A. / Kotaka, M. / Kong, R. / Sun, H. / Qureshi, I. / Bricogne, G. / Liang, Z.X. / Lescar, J.
External linksJ. Mol. Biol. / PubMed:20888341
MethodsX-ray diffraction
Resolution2.1 - 2.9 Å
Structure data

PDB-2xem:
Induced-fit and allosteric effects upon polyene binding revealed by crystal structures of the Dynemicin thioesterase
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2xfl:
Induced-fit and allosteric effects upon polyene binding revealed by crystal structures of the Dynemicin thioesterase
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-SSV:
(3E,5E,7E,9E,11E,13E)-pentadeca-3,5,7,9,11,13-hexaen-2-one

ChemComp-HOH:
WATER

Source
  • micromonospora chersina (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / POLYKETIDE BIOSYNTHESIS / ENEDIYNE ANTITUMOR AGENT / THIOESTERASE / HYDROLASE / ENEDIYNE / HOT-DOG FOLD

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