› 4rwu

X-ray diffraction
1.25Å resolution

J-domain of Sis1 protein, Hsp40 co-chaperone from Saccharomyces cerevisiae

Released:
DOI: 10.2210/pdb4rwu/pdb
PDB entry 4rwu coloured by chain, front view.
PDB entry 4rwu coloured by chain, side view.
PDB entry 4rwu coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Roles of intramolecular and intermolecular interactions in functional regulation of the Hsp70 J-protein co-chaperone Sis1.
Yu HY, Ziegelhoffer T, Osipiuk J, Ciesielski SJ, Baranowski M, Zhou M, Joachimiak A, Craig EA
J Mol Biol 427 1632-43 (2015)
PMID: 25687964

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein SIS1 Chain: A
Molecule details ›
Chain: A
Length: 92 amino acids
Theoretical weight: 9.92 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P25294 (Residues: 1-89; Coverage: 25%)
Gene names: N2879, SIS1, YNL007C
Sequence domains: DnaJ domain
Structure domains: DnaJ domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 31.645Å b: 43.564Å c: 65.572Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.123 0.122 0.149
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

How Do J-Proteins Get Hsp70 to Do So Many Different Things?
Craig et al. (2017)
2 more

7 mentions without citation

Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes.
Nillegoda et al. (2017)
6 more