› 1l2p

X-ray diffraction
1.55Å resolution

ATP Synthase b Subunit Dimerization Domain

Released:
DOI: 10.2210/pdb1l2p/pdb
PDB entry 1l2p coloured by chain, front view.
PDB entry 1l2p coloured by chain, side view.
PDB entry 1l2p coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain.
Del Rizzo PA, Bi Y, Dunn SD, Shilton BH
Biochemistry 41 6875-84 (2002)
PMID: 12022893

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-142033 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP synthase subunit b Chain: A
Molecule details ›
Chain: A
Length: 61 amino acids
Theoretical weight: 7.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABA0 (Residues: 62-122; Coverage: 39%)
Gene names: JW3714, atpF, b3736, papF, uncF
Sequence domains: ATP synthase B/B' CF(0)
Structure domains: F1F0 ATP synthase subunit B, membrane domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21212
Unit cell:
a: 35.7Å b: 40.76Å c: 42.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.285 0.282 0.313
Expression system: Escherichia coli

Quick links

Citations

11 review citations

ATP synthesis driven by proton transport in F1F0-ATP synthase.
Weber et al. (2003)
10 more

8 mentions without citation

Biological Nanomotors with a Revolution, Linear, or Rotation Motion Mechanism.
Guo et al. (2016)
7 more