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Structure paper

TitleStructural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.
Journal, issue, pagesMol. Cell, Vol. 53, Page 330-343, Year 2014
Publish dateJan 9, 2013 (structure data deposition date)
AuthorsLavery, L.A. / Partridge, J.R. / Ramelot, T.A. / Elnatan, D. / Kennedy, M.A. / Agard, D.A.
External linksMol. Cell / PubMed:24462206
MethodsX-ray diffraction
Resolution1.749 - 2.352 Å
Structure data

PDB-4ipe:
Crystal structure of mitochondrial Hsp90 (TRAP1) with AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 2.289 Å

PDB-4ivg:
Crystal structure of mitochondrial Hsp90 (TRAP1) NTD-Middle domain dimer with AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 1.749 Å

PDB-4iyn:
Structure of mitochondrial Hsp90 (TRAP1) with ADP-ALF4-
Method: X-RAY DIFFRACTION / Resolution: 2.312 Å

PDB-4j0b:
Structure of mitochondrial Hsp90 (TRAP1) with ADP-BeF3
Method: X-RAY DIFFRACTION / Resolution: 2.352 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-CO:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

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

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

Source
  • danio rerio (zebrafish)
KeywordsCHAPERONE / ATPase / ATP binding / Mitochondria / ATPase chaperone

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