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Structure paper

TitleAMPylation targets the rate-limiting step of BiP's ATPase cycle for its functional inactivation.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateMay 30, 2017 (structure data deposition date)
AuthorsPreissler, S. / Rohland, L. / Yan, Y. / Chen, R. / Read, R.J. / Ron, D.
External linksElife / PubMed:29064368
MethodsX-ray diffraction
Resolution1.59 - 2 Å
Structure data

PDB-5o4p:
Crystal structure of AMPylated GRP78
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-6eob:
Crystal structure of AMPylated GRP78 in apo form (Crystal form 1)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6eoc:
Crystal structure of AMPylated GRP78 in apo form (Crystal form 2)
Method: X-RAY DIFFRACTION / Resolution: 1.67 Å

PDB-6eoe:
Crystal structure of AMPylated GRP78 with nucleotide
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

PDB-6eof:
Crystal structure of AMPylated GRP78 in ADP state
Method: X-RAY DIFFRACTION / Resolution: 1.59 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-FLC:
CITRATE ANION

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • cricetulus griseus (Chinese hamster)
KeywordsATP BINDING PROTEIN / Bip/GRP78 / AMPylation / CHAPERONE / GRP78 / Bip / apo / ADP

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