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Structure paper

TitleStructural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor.
Journal, issue, pagesBiochem. J., Vol. 438, Page 447-455, Year 2011
Publish dateJan 22, 2011 (structure data deposition date)
AuthorsYan, M. / Li, J. / Sha, B.
External linksBiochem. J. / PubMed:21675960
MethodsX-ray diffraction
Resolution1.8 - 2.31 Å
Structure data

PDB-3qfp:
Crystal structure of yeast Hsp70 (Bip/Kar2) ATPase domain
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

PDB-3qfu:
Crystal structure of Yeast Hsp70 (Bip/kar2) complexed with ADP
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3qml:
The structural analysis of Sil1-Bip complex reveals the mechanism for Sil1 to function as a novel nucleotide exchange factor
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

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

ChemComp-MG:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCHAPERONE / Hsp70 / Kar2 / Bip / CHAPERONE/PROTEIN TRANSPORT / Armadillo like repeats / CHAPERONE-PROTEIN TRANSPORT complex

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