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Structure paper

TitleStereospecific proton transfer by a mobile catalyst in mammalian fructose-1,6-bisphosphate aldolase
Journal, issue, pagesJ. Biol. Chem., Vol. 282, Page 31028-31037, Year 2007
Publish dateAug 6, 2007 (structure data deposition date)
AuthorsSt-Jean, M. / Sygusch, J.
External linksJ. Biol. Chem. / PubMed:17728250
MethodsX-ray diffraction
Resolution1.88 - 2.22 Å
Structure data

PDB-2qut:
Dihydroxyacetone phosphate enamine intermediate in fructose-1,6-bisphosphate aldolase from rabbit muscle
Method: X-RAY DIFFRACTION / Resolution: 1.88 Å

PDB-2quu:
Dihydroxyacetone phosphate Schiff base intermediate in mutant fructose-1,6-bisphosphate aldolase from rabbit muscle
Method: X-RAY DIFFRACTION / Resolution: 1.98 Å

PDB-2quv:
Phosphate ions in fructose-1,6-bisphosphate aldolase from rabbit muscle
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

Chemicals

ChemComp-13P:
1,3-DIHYDROXYACETONEPHOSPHATE

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • oryctolagus cuniculus (rabbit)
KeywordsLYASE / aldolase / substrate / enamine / intermediate / covalent / Acetylation / Glycolysis / Phosphorylation / Schiff base / mutant / protonated imine / phosphate ions

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