› 4ipe

X-ray diffraction
2.29Å resolution

Crystal structure of mitochondrial Hsp90 (TRAP1) with AMPPNP

Released:
DOI: 10.2210/pdb4ipe/pdb
PDB entry 4ipe coloured by chain, front view.
PDB entry 4ipe coloured by chain, side view.
PDB entry 4ipe coloured by chain, top view.
Source organism: Danio rerio
Primary publication:
Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.
Lavery LA, Partridge JR, Ramelot TA, Elnatan D, Kennedy MA, Agard DA
Mol Cell 53 330-43 (2014)
PMID: 24462206

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108806 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine kinase/HSP90-like ATPase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 719 amino acids
Theoretical weight: 82.23 KDa
Source organism: Danio rerio
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A8WFV1 (Residues: 1-719; Coverage: 100%)
Gene names: fc85a11, trap1, wu:fc85a11
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ANP 2 x ANP
Ligand MG 2 x MG
Ligand CO 4 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 177.977Å b: 96.362Å c: 125.153Å
α: 90° β: 134.34° γ: 90°
R-values:
R R work R free
0.181 0.18 0.225
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

27 review citations

The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology.
Bernardi et al. (2015)
26 more

17 mentions without citation

Structure, Function, and Regulation of the Hsp90 Machinery.
Biebl et al. (2019)
16 more