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Structure paper

TitleStructural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase.
Journal, issue, pagesBiochemistry, Vol. 47, Page 8016-8025, Year 2008
Publish dateApr 21, 2008 (structure data deposition date)
AuthorsReger, A.S. / Wu, R. / Dunaway-Mariano, D. / Gulick, A.M.
External linksBiochemistry / PubMed:18620418
MethodsX-ray diffraction
Resolution2 - 2.25 Å
Structure data

PDB-3cw8:
4-Chlorobenzoyl-CoA Ligase/Synthetase, bound to 4CBA-Adenylate
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-3cw9:
4-Chlorobenzoyl-CoA Ligase/Synthetase in the Thioester-forming Conformation, bound to 4-chlorophenacyl-CoA
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-00A:
5'-O-[(S)-{[(4-chlorophenyl)carbonyl]oxy}(hydroxy)phosphoryl]adenosine

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-NO3:
NITRATE ION

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-01A:
4-Chlorophenacyl-coenzyme A

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

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