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Structure paper

TitleLigand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone.
Journal, issue, pagesJ. Biol. Chem., Vol. 279, Page 46162-46171, Year 2004
Publish dateMay 20, 2004 (structure data deposition date)
AuthorsImmormino, R.M. / Dollins, D.E. / Shaffer, P.L. / Soldano, K.L. / Walker, M.A. / Gewirth, D.T.
External linksJ. Biol. Chem. / PubMed:15292259
MethodsX-ray diffraction
Resolution1.87 - 2.2 Å
Structure data

PDB-1tbw:
Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-1tc0:
Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1tc6:
Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-Complex
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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

Source
  • canis lupus familiaris (dog)
KeywordsCHAPERONE / GRP94 / HSP90 / AMP / Bergrat / Endoplasmic reticulum / ATP / Bergerat / ADP

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