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Structure paper

TitleSequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase.
Journal, issue, pagesJ. Biol. Chem., Vol. 275, Page 27186-27196, Year 2000
Publish dateMay 17, 2000 (structure data deposition date)
AuthorsBarycki, J.J. / O'Brien, L.K. / Strauss, A.W. / Banaszak, L.J.
External linksPubMed:10840044
MethodsX-ray diffraction
Resolution1.8 - 2.4 Å
Structure data

PDB-1f0y:
L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH ACETOACETYL-COA AND NAD+
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1f12:
L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH 3-HYDROXYBUTYRYL-COA
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1f14:
L-3-HYDROXYACYL-COA DEHYDROGENASE (APO)
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-1f17:
L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH NADH
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-CAA:
ACETOACETYL-COENZYME A

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-HOH:
WATER

ChemComp-3HC:
3-HYDROXYBUTANOYL-COENZYME A

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / Abortive ternary complex / L-3-hydroxyacyl-CoA complexed with 3-hydroxybutyryl-CoA / L-3-hydroxyacyl-CoA (apoenzyme) / L-3-hydroxyacyl-CoA dehydrogenase complexed with NADH

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