› 1ijp

Solution NMR

Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase

Released:
DOI: 10.2210/pdb1ijp/pdb
PDB entry 1ijp coloured by chain, ensemble of 10 models, front view.
PDB entry 1ijp coloured by chain, ensemble of 10 models, side view.
PDB entry 1ijp coloured by chain, ensemble of 10 models, top view.
Source organism: Escherichia coli
Primary publication:
Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices.
Dmitriev OY, Fillingame RH
J Biol Chem 276 27449-54 (2001)
PMID: 11331283

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159499 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP synthase subunit c Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 8.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P68699 (Residues: 1-79; Coverage: 100%)
Gene names: JW3715, atpE, b3737, papH, uncE
Sequence domains: ATP synthase subunit C
Structure domains: F1F0 ATP synthase subunit C

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

Quick links

Citations

1 review citation

Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.
Rainey et al. (2006)
4 other articles

2 mentions without citation

Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.
Cieplak AS. (2017)
1 more