› 2o29

X-ray diffraction
1.8Å resolution

Spectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-BR Complex

Released:
DOI: 10.2210/pdb2o29/pdb
PDB entry 2o29 coloured by chain, front view.
PDB entry 2o29 coloured by chain, side view.
PDB entry 2o29 coloured by chain, top view.
Source organism: Aequorea victoria
Primary publication:
Spectroscopic and structural study of proton and halide ion cooperative binding to gfp.
Arosio D, Garau G, Ricci F, Marchetti L, Bizzarri R, Nifosì R, Beltram F
Biophys J 93 232-44 (2007)
PMID: 17434942

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154537 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Green fluorescent protein Chain: A
Molecule details ›
Chain: A
Length: 242 amino acids
Theoretical weight: 27.52 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P42212 (Residues: 2-238; Coverage: 100%)
Gene name: GFP
Sequence domains: Green fluorescent protein
Structure domains: Green fluorescent protein

Ligands and Environments

1 bound ligand:
Ligand BR 4 x BR
1 modified residue:
Ligand CRO 1 x CRO

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 51.144Å b: 62.852Å c: 69.172Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.208
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Genetically Encoded Fluorescent Biosensors Illuminate the Spatiotemporal Regulation of Signaling Networks.
Greenwald et al. (2018)
9 more

1 mention without citation

Spectroscopic and structural study of proton and halide ion cooperative binding to gfp.
Arosio et al. (2007)