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TitleThe Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2.
Journal, issue, pagesMol. Cell, Vol. 74, Page 73-87.e8, Year 2019
Publish dateAug 21, 2018 (structure data deposition date)
AuthorsSchopf, F.H. / Huber, E.M. / Dodt, C. / Lopez, A. / Biebl, M.M. / Rutz, D.A. / Muhlhofer, M. / Richter, G. / Madl, T. / Sattler, M. ...Schopf, F.H. / Huber, E.M. / Dodt, C. / Lopez, A. / Biebl, M.M. / Rutz, D.A. / Muhlhofer, M. / Richter, G. / Madl, T. / Sattler, M. / Groll, M. / Buchner, J.
External linksMol. Cell / PubMed:30876805
MethodsX-ray diffraction
Resolution1.55 - 2.8 Å
Structure data

PDB-6hfm:
Hsp90 co-chaperone Cns1 C-domain from Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-6hfo:
Human Hsp90 co-chaperone TTC4 C-domain
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-6hft:
Hsp90 co-chaperone Cns1 from Saccharomyces cerevisiae (delta69)
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • homo sapiens (human)
KeywordsCHAPERONE / unique fold / wheel domain / Hsp90 co-chaperone / two-domain fold / TPR domain

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