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Structure paper

TitleBiochemical and Crystallographic Analysis of Substrate Binding and Conformational Changes in Acetyl-CoA Synthetase.
Journal, issue, pagesBiochemistry, Vol. 46, Page 6536-6546, Year 2007
Publish dateMar 6, 2007 (structure data deposition date)
AuthorsReger, A.S. / Carney, J.M. / Gulick, A.M.
External linksBiochemistry / PubMed:17497934
MethodsX-ray diffraction
Resolution2.11 - 2.58 Å
Structure data

PDB-2p20:
Acetyl-CoA Synthetase, R584A mutation
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

PDB-2p2b:
Acetyl-CoA Synthetase, V386A mutation
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2p2f:
Acetyl-CoA Synthetase, wild-type with acetate, AMP, and CoA bound
Method: X-RAY DIFFRACTION / Resolution: 2.58 Å

PDB-2p2j:
Acetyl-CoA Synthetase, K609A mutation
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2p2m:
Acetyl-CoA Synthetase, R194A mutation
Method: X-RAY DIFFRACTION / Resolution: 2.11 Å

PDB-2p2q:
Acetyl-CoA Synthetase, R584E mutation
Method: X-RAY DIFFRACTION / Resolution: 2.42 Å

Chemicals

ChemComp-PRX:
ADENOSINE-5'-MONOPHOSPHATE-PROPYL ESTER

ChemComp-HOH:
WATER

ChemComp-COA:
COENZYME A

ChemComp-ACT:
ACETATE ION

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • salmonella typhimurium (bacteria)
KeywordsLIGASE / Adenylate-forming enzymes / Domain Alternation / Acyl-CoA ligase

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