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Structure paper

TitleStructure of the Hsp110:Hsc70 nucleotide exchange machine
Journal, issue, pagesMol. Cell, Vol. 31, Page 232-243, Year 2008
Publish dateFeb 7, 2008 (structure data deposition date)
AuthorsSchuermann, J.P. / Jiang, J. / Cuellar, J. / Llorca, O. / Wang, L. / Gimenez, L.E. / Jin, S. / Taylor, A.B. / Demeler, B. / Morano, K.A. ...Schuermann, J.P. / Jiang, J. / Cuellar, J. / Llorca, O. / Wang, L. / Gimenez, L.E. / Jin, S. / Taylor, A.B. / Demeler, B. / Morano, K.A. / Hart, P.J. / Valpuesta, J.M. / Lafer, E.M. / Sousa, R.
External linksMol. Cell / PubMed:18550409
MethodsX-ray diffraction
Resolution3.115 Å
Structure data

PDB-3c7n:
Structure of the Hsp110:Hsc70 Nucleotide Exchange Complex
Method: X-RAY DIFFRACTION / Resolution: 3.115 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

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

ChemComp-CL:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • bos taurus (domestic cattle)
KeywordsCHAPERONE/CHAPERONE / chaperone / HSP110 / HSP70 / HSC70 / molecular chaperone / ATP state / acetylation / ATP-binding / ADP / calmodulin binding / cytoplasm / mucleotide binding / phosphorylation / stress response / Calmodulin-binding / Nucleotide-binding / Phosphoprotein / Nucleus / TRANSCRIPTION / CHAPERONE-CHAPERONE COMPLEX

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