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Structure paper

TitleStructural and biochemical studies of a fluoroacetyl-CoA-specific thioesterase reveal a molecular basis for fluorine selectivity.
Journal, issue, pagesBiochemistry, Vol. 49, Page 9269-9279, Year 2010
Publish dateOct 3, 2010 (structure data deposition date)
AuthorsWeeks, A.M. / Coyle, S.M. / Jinek, M. / Doudna, J.A. / Chang, M.C.
External linksBiochemistry / PubMed:20836570
MethodsX-ray diffraction
Resolution1.85 - 2.46 Å
Structure data

PDB-3p2q:
Crystal structure of the fluoroacetyl-CoA-specific thioesterase, FlK
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3p2r:
Crystal structure of the fluoroacetyl-CoA-specific thioesterase FlK in complex with fluoroacetate
Method: X-RAY DIFFRACTION / Resolution: 2.46 Å

PDB-3p2s:
Crystal structure of the fluoroacetyl-CoA-specific thioesterase FlK in an open conformation
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-3p3f:
Crystal structure of the F36A mutant of the fluoroacetyl-CoA-specific thioesterase FlK
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3p3i:
Crystal structure of the F36A mutant of the fluoroacetyl-CoA-specific thioesterase FlK in complex with fluoroacetate and CoA
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-FAH:
fluoroacetic acid

ChemComp-COA:
COENZYME A

Source
  • streptomyces cattleya (bacteria)
KeywordsHYDROLASE / hot dog-fold / thioesterase

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