2oen

X-ray diffraction
3.17Å resolution

Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose-6-phosphate and fructose-1,6-bisphosphate

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-130648 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Catabolite control protein A Chain: G
Molecule details ›
Chain: G
Length: 280 amino acids
Theoretical weight: 30.99 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P46828 (Residues: 53-332; Coverage: 84%)
Gene name: ccpA
Sequence domains: Periplasmic binding protein-like domain
Structure domains: Rossmann fold
Phosphocarrier protein HPr Chain: L
Molecule details ›
Chain: L
Length: 88 amino acids
Theoretical weight: 9.21 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O69250 (Residues: 1-88; Coverage: 100%)
Gene name: ptsH
Sequence domains: PTS HPr component phosphorylation site
Structure domains: HPr-like

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P41212
Unit cell:
a: 69.33Å b: 69.33Å c: 229.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.279 0.278 0.318
Expression system: Escherichia coli BL21(DE3)