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Structure paper

TitleStructures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones.
Journal, issue, pagesMol. Cell, Vol. 28, Page 41-56, Year 2007
Publish dateNov 29, 2006 (structure data deposition date)
AuthorsDollins, D.E. / Warren, J.J. / Immormino, R.M. / Gewirth, D.T.
External linksMol. Cell / PubMed:17936703
MethodsX-ray diffraction
Resolution2.4 - 3.4 Å
Structure data

PDB-2o1t:
Structure of Middle plus C-terminal domains (M+C) of GRP94
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-2o1u:
Structure of full length GRP94 with AMP-PNP bound
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2o1v:
Structure of full length GRP94 with ADP bound
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

PDB-2o1w:
Structure of N-terminal plus middle domains (N+M) of GRP94
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-HOH:
WATER

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

Source
  • canis lupus familiaris (dog)
KeywordsCHAPERONE / GRP94 / HSP82 / HSP90 / HTPG / GP96 / endoplasmin / AMP-PNP / ADP

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