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Structure paper

TitleStructure and function of Hip, an attenuator of the Hsp70 chaperone cycle.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 20, Page 929-935, Year 2013
Publish dateFeb 14, 2013 (structure data deposition date)
AuthorsLi, Z. / Hartl, F.U. / Bracher, A.
External linksNat. Struct. Mol. Biol. / PubMed:23812373
MethodsX-ray diffraction
Resolution1.1 - 2.8 Å
Structure data

PDB-4j8c:
Crystal structure of the dimerization domain of Hsc70-interacting protein
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

PDB-4j8d:
Middle domain of Hsc70-interacting protein, crystal form II
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-4j8e:
Middle domain of Hsc70-interacting protein, crystal form I
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-4j8f:
Crystal structure of a fusion protein containing the NBD of Hsp70 and the middle domain of Hip
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

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

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-IOD:
IODIDE ION

Source
  • rattus norvegicus (Norway rat)
  • homo sapiens (human)
KeywordsCHAPERONE / alpha helical dimer / Co-chaperone / cytosol / tetratricopeptide repeat / solenoid / actin-like fold / nucleotide binding domain / Molecular chaperone complex

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