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Structure paper

TitleMechanism of displacement of a catalytically essential loop from the active site of mammalian fructose-1,6-bisphosphatase.
Journal, issue, pagesBiochemistry, Vol. 52, Page 5206-5216, Year 2013
Publish dateNov 20, 2005 (structure data deposition date)
AuthorsGao, Y. / Iancu, C.V. / Mukind, S. / Choe, J.Y. / Honzatko, R.B.
External linksBiochemistry / PubMed:23844654
MethodsX-ray diffraction
Resolution1.8 - 2.7 Å
Structure data

PDB-2f3b:
Mechanism of displacement of a catalytically essential loop from the active site of fructose-1,6-bisphosphatase
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2f3d:
Mechanism of displacement of a catalytically essential loop from the active site of fructose-1,6-bisphosphatase
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

PDB-4kxp:
Crystal Structure of AMP complexes of Porcine Liver Fructose-1,6-bisphosphatase Mutant I10D in T-state
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-F6P:
6-O-phosphono-beta-D-fructofuranose

ChemComp-PO4:
PHOSPHATE ION

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-MG:
Unknown entry

Source
  • sus scrofa (pig)
KeywordsHYDROLASE / allostery / allosteric regulation / loop diengagement / enzyme catalysis / FBPase / fructose-1 / 6-bisphosphatase / loop displacement / Allosteric Enzymes / T-state

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