› 3c7n

X-ray diffraction
3.12Å resolution

Structure of the Hsp110:Hsc70 Nucleotide Exchange Complex

Released:
DOI: 10.2210/pdb3c7n/pdb
PDB 3c7n coloured by chain and viewed from the front.
PDB 3c7n coloured by chain and viewed from the side.
PDB 3c7n coloured by chain and viewed from the top.
Source organisms:
Primary publication:
Structure of the Hsp110:Hsc70 nucleotide exchange machine.
Schuermann JP, Jiang J, Cuellar J, Llorca O, Wang L, Gimenez LE, Jin S, Taylor AB, Demeler B, Morano KA, Hart PJ, Valpuesta JM, Lafer EM, Sousa R
Mol Cell 31 232-43 (2008)
PMID: 18550409

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Heat shock protein homolog SSE1 Chain: A
Molecule details ›
Chain: A
Length: 668 amino acids
Theoretical weight: 74.54 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P32589 (Residues: 1-666; Coverage: 96%)
Gene names: LPG3C, MSI3, SSE1, YPL106C
Sequence domains: Hsp70 protein
Structure domains:
Heat shock cognate 71 kDa protein Chain: B
Molecule details ›
Chain: B
Length: 554 amino acids
Theoretical weight: 61.08 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19120 (Residues: 1-554; Coverage: 85%)
Gene names: HSC70, HSPA8
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand MG 2 x MG
Ligand SO4 4 x SO4
Ligand BEF 1 x BEF
Ligand ADP 2 x ADP
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21212
Unit cell:
a: 123.533Å b: 169.501Å c: 87.724Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.224 0.283
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

33 review citations

Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome.
Abildgaard et al. (2020)
32 more

24 mentions without citation

Targeting Allosteric Control Mechanisms in Heat Shock Protein 70 (Hsp70).
Li et al. (2016)
23 more