› 2e5u

Solution NMR

C-terminal domain of Epsilon subunit of F1F0-ATP synthase from the Thermophilic Bacillus PS3

Released:
DOI: 10.2210/pdb2e5u/pdb
PDB entry 2e5u coloured by chain, ensemble of 20 models, front view.
PDB entry 2e5u coloured by chain, ensemble of 20 models, side view.
PDB entry 2e5u coloured by chain, ensemble of 20 models, top view.
Source organism: Bacillus sp. PS3
Primary publication:
Structures of the thermophilic F1-ATPase epsilon subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1.
Yagi H, Kajiwara N, Tanaka H, Tsukihara T, Kato-Yamada Y, Yoshida M, Akutsu H
Proc Natl Acad Sci U S A 104 11233-8 (2007)
PMID: 17581881

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-177356 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP synthase epsilon chain Chain: A
Molecule details ›
Chain: A
Length: 40 amino acids
Theoretical weight: 4.74 KDa
Source organism: Bacillus sp. PS3
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5KUJ4 (Residues: 88-127; Coverage: 30%)
Gene names: GK3357, atpC
Sequence domains: ATP synthase, Delta/Epsilon chain, long alpha-helix domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Genetically encodable fluorescent biosensors for tracking signaling dynamics in living cells.
Newman et al. (2011)
12 more

4 mentions without citation

Dynamic mechanisms driving conformational conversions of the β and ε subunits involved in rotational catalysis of F1-ATPase.
Akutsu H. (2017)
3 more