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TitleRational redesign of the 4-chlorobenzoate binding site of 4-chlorobenzoate: coenzyme a ligase for expanded substrate range.
Journal, issue, pagesBiochemistry, Vol. 46, Page 14487-14499, Year 2007
Publish dateAug 9, 2007 (structure data deposition date)
AuthorsWu, R. / Reger, A.S. / Cao, J. / Gulick, A.M. / Dunaway-Mariano, D.
External linksBiochemistry / PubMed:18027984
MethodsX-ray diffraction
Resolution2.5 - 2.76 Å
Structure data

PDB-2qvx:
4-Chlorobenzoyl-CoA Ligase/Synthetase, I303G mutation, bound to 3-Chlorobenzoate
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-2qvy:
4-Chlorobenzoyl-CoA Ligase/Synthetase, I303G mutation, bound to 3,4-Dichlorobenzoate
Method: X-RAY DIFFRACTION / Resolution: 2.76 Å

PDB-2qvz:
4-Chlorobenzoyl-CoA Ligase/Synthetase, I303A mutation, bound to 3-Chlorobenzoate
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-2qw0:
4-Chlorobenzoyl-CoA Ligase/Synthetase, I303A mutation, bound to 3,4 Dichlorobenzoate
Method: X-RAY DIFFRACTION / Resolution: 2.56 Å

Chemicals

ChemComp-3BZ:
3-chlorobenzoate

ChemComp-HOH:
WATER

ChemComp-34Z:
3,4-dichlorobenzoate

Source
  • alcaligenes sp. (bacteria)
KeywordsLIGASE / Adenylate-forming enzymes / Acyl-CoA ligase

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