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TitleThe Sulfur Atoms of the Substrate Coa and the Catalytic Cysteine are Required for a Productive Mode of Substrate Binding in Bacterial Biosynthetic Thiolase, a Thioester-Dependent Enzyme.
Journal, issue, pagesFEBS J., Vol. 275, Page 6136-, Year 2008
Publish dateMay 19, 2008 (structure data deposition date)
AuthorsMerilainen, G. / Schmitz, W. / Wierenga, R.K. / Kursula, P.
External linksFEBS J. / PubMed:19016856
MethodsX-ray diffraction
Resolution1.51 - 2.65 Å
Structure data

PDB-2vtz:
Biosynthetic thiolase from Z. ramigera. Complex of the C89A mutant with coenzyme A.
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2vu0:
Biosynthetic thiolase from Z. ramigera. Complex of the oxidised enzyme with coenzyme A.
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-2vu1:
Biosynthetic thiolase from Z. ramigera. Complex of with O-pantheteine- 11-pivalate.
Method: X-RAY DIFFRACTION / Resolution: 1.51 Å

PDB-2vu2:
Biosynthetic thiolase from Z. ramigera. Complex with S-pantetheine-11- pivalate.
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

Chemicals

ChemComp-COA:
COENZYME A

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-OPI:
PANTOTHENYL-AMINOETHANOL-11-PIVALIC ACID

ChemComp-NA:
Unknown entry

ChemComp-PN5:
(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate

Source
  • zoogloea ramigera (bacteria)
KeywordsTRANSFERASE / ACYLTRANSFERASE / PHB BIOSYNTHESIS / THIOLASE FOLD

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