› 1bsn

Solution NMR

SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX

Released:
DOI: 10.2210/pdb1bsn/pdb
PDB entry 1bsn coloured by chain, front view.
PDB entry 1bsn coloured by chain, side view.
PDB entry 1bsn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex.
Wilkens S, Capaldi RA
J Biol Chem 273 26645-51 (1998)
PMID: 9756905

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP synthase epsilon chain Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 14.96 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6E6 (Residues: 2-139; Coverage: 99%)
Gene names: JW3709, atpC, b3731, papG, uncC
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Escherichia coli

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Citations

10 review citations

ATP synthase--a marvellous rotary engine of the cell.
Yoshida et al. (2001)
9 more

9 mentions without citation

Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.
Krah et al. (2018)
8 more