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Structure paper

TitleStructures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition.
Journal, issue, pagesJ. Mol. Biol., Vol. 429, Page 3075-3089, Year 2017
Publish dateJul 10, 2017 (structure data deposition date)
AuthorsYuan, M. / Vasquez-Valdivieso, M.G. / McNae, I.W. / Michels, P.A.M. / Fothergill-Gilmore, L.A. / Walkinshaw, M.D.
External linksJ. Mol. Biol. / PubMed:28882541
MethodsX-ray diffraction
Resolution2.41 - 2.8 Å
Structure data

PDB-5oey:
Crystal structure of Leishmania major fructose-1,6-bisphosphatase in holo form.
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5oez:
Crystal structure of Leishmania major fructose-1,6-bisphosphatase in apo form.
Method: X-RAY DIFFRACTION / Resolution: 2.41 Å

PDB-5ofu:
Crystal structure of Leishmania major fructose-1,6-bisphosphatase in T-state.
Method: X-RAY DIFFRACTION / Resolution: 2.62 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-MN:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-CIT:
CITRIC ACID

ChemComp-HOH:
WATER

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

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

ChemComp-CL:
Unknown entry

Source
  • leishmania major (eukaryote)
KeywordsHYDROLASE / Allostery / Gluconeogenesis / TRANSFERASE

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