› 1l6t

Solution NMR

STRUCTURE OF ALA24/ASP61 TO ASP24/ASN61 SUBSTITUTED SUBUNIT C OF ESCHERICHIA COLI ATP SYNTHASE

Released:
DOI: 10.2210/pdb1l6t/pdb
PDB entry 1l6t coloured by chain, ensemble of 10 models, front view.
PDB entry 1l6t coloured by chain, ensemble of 10 models, side view.
PDB entry 1l6t coloured by chain, ensemble of 10 models, top view.
Source organism: Escherichia coli
Primary publication:
Structure of Ala24/Asp61 --> Asp24/Asn61 substituted subunit c of Escherichia coli ATP synthase: implications for the mechanism of proton transport and rotary movement in the F0 complex.
Dmitriev OY, Abildgaard F, Markley JL, Fillingame RH
Biochemistry 41 5537-47 (2002)
PMID: 11969414

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: 8.3 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

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Citations

3 review citations

Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
Fillingame et al. (2003)
2 more