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TitleMitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 113, Page 2952-2957, Year 2016
Publish dateDec 2, 2015 (structure data deposition date)
AuthorsSung, N. / Lee, J. / Kim, J.H. / Chang, C. / Joachimiak, A. / Lee, S. / Tsai, F.T.
External linksProc. Natl. Acad. Sci. USA / PubMed:26929380
MethodsX-ray diffraction
Resolution1.82 - 1.85 Å
Structure data

PDB-5f3k:
X-Ray Crystallographic Structure of hTrap1 N-terminal Domain-apo
Method: X-RAY DIFFRACTION / Resolution: 1.82 Å

PDB-5f5r:
TRAP1N-ADPNP
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-HOH:
WATER

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

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCHAPERONE / Trap1 / Hsp90 / apo / ATPase / GHKL ATPase

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