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Structure paper

TitleThe catalytic cycle of biosynthetic thiolase: A conformational journey of an acetyl group through four binding modes and two oxyanion holes
Journal, issue, pagesBiochemistry, Vol. 41, Page 15543-15556, Year 2002
Publish dateJun 20, 2002 (structure data deposition date)
AuthorsKursula, P. / Ojala, J. / Lambeir, A.-M. / Wierenga, R.K.
External linksBiochemistry / PubMed:12501183
MethodsX-ray diffraction
Resolution1.7 - 1.95 Å
Structure data

PDB-1m1o:
Crystal structure of biosynthetic thiolase, C89A mutant, complexed with acetoacetyl-CoA
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-1m1t:
Biosynthetic thiolase, Q64A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.94 Å

PDB-1m3k:
biosynthetic thiolase, inactive C89A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1m3z:
Biosynthetic thiolase, C89A mutant, complexed with acetyl coenzyme A
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-1m4s:
Biosynthetic thiolase, Cys89 acetylated, unliganded form
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-1m4t:
Biosynthetic thiolase, Cys89 butyrylated
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-CAA:
ACETOACETYL-COENZYME A

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-ACO:
ACETYL COENZYME *A

Source
  • zoogloea ramigera (bacteria)
KeywordsTRANSFERASE / thiolase fold / acetylated intermediate / butyrylated intermediate

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