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Structure paper

TitleStructures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD.
Journal, issue, pagesNat Commun, Vol. 12, Page 5004-5004, Year 2021
Publish dateDec 12, 2020 (structure data deposition date)
AuthorsPerera, L.A. / Preissler, S. / Zaccai, N.R. / Prevost, S. / Devos, J.M. / Haertlein, M. / Ron, D.
External linksNat Commun / PubMed:34408154
MethodsX-ray diffraction
Resolution1.7 - 1.87 Å
Structure data

PDB-7b7z:
DeAMPylation complex of monomeric FICD and AMPylated BiP (state 1)
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-7b80:
DeAMPylation complex of monomeric FICD and AMPylated BiP (state 2)
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-K:
Unknown entry

ChemComp-P33:
3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL / precipitant*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • cricetulus griseus (Chinese hamster)
  • homo sapiens (human)
KeywordsHYDROLASE / FICD / Fic / HYPE / BiP / Grp78 / AMPylation / deAMPylation / deAMPylase / ER stress / Complex / adenylation / adenylylation / Hsp70 / chaperone / transferase

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