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Structure paper

TitleA structure of substrate-bound Synaptojanin1 provides new insights in its mechanism and the effect of disease mutations.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateAug 11, 2020 (structure data deposition date)
AuthorsPaesmans, J. / Martin, E. / Deckers, B. / Berghmans, M. / Sethi, R. / Loeys, Y. / Pardon, E. / Steyaert, J. / Verstreken, P. / Galicia, C. / Versees, W.
External linksElife / PubMed:33349335
MethodsX-ray diffraction
Resolution2.3 - 2.73 Å
Structure data

PDB-7a0v:
Crystal structure of the 5-phosphatase domain of Synaptojanin1 in complex with a nanobody
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-7a17:
Crystal structure of the 5-phosphatase domain of Synaptojanin1 bound to its substrate diC8-PI(3,4,5)P3 in complex with a nanobody
Method: X-RAY DIFFRACTION / Resolution: 2.73 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-IP9:
(2R)-3-{[(R)-{[(1S,2S,3R,4S,5S,6S)-2,6-dihydroxy-3,4,5-tris(phosphonooxy)cyclohexyl]oxy}(hydroxy)phosphoryl]oxy}propane

Source
  • homo sapiens (human)
  • lama glama (llama)
KeywordsHYDROLASE / Inositol polyphosphate 5-phosphatase / Phosphoinositide / Parkinson's disease / Epilepsy / Enzyme-substrate complex / Catalytic Mechanism

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