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Structure paper

TitleT-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structure.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 72, Page 536-550, Year 2016
Publish dateNov 17, 2015 (structure data deposition date)
AuthorsBarciszewski, J. / Wisniewski, J. / Kolodziejczyk, R. / Jaskolski, M. / Rakus, D. / Dzugaj, A.
External linksActa Crystallogr D Struct Biol / PubMed:27050133
MethodsX-ray diffraction
Resolution1.67 - 2.989 Å
Structure data

PDB-5et5:
Human muscle fructose-1,6-bisphosphatase in active R-state
Method: X-RAY DIFFRACTION / Resolution: 1.67 Å

PDB-5et6:
Human muscle fructose-1,6-bisphosphatase in inactive T-state in complex with AMP
Method: X-RAY DIFFRACTION / Resolution: 1.845 Å

PDB-5et7:
Human muscle fructose-1,6-bisphosphatase in inactive T-state
Method: X-RAY DIFFRACTION / Resolution: 2.989 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • homo sapiens (human)
KeywordsHYDROLASE / carbohydrate metabolism / glyconeogenesis / muscle / FBPase / R-state / Leucine lock / Asp187 / T-state / AMP

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