› 2q8m

X-ray diffraction
2.05Å resolution

T-like Fructose-1,6-bisphosphatase from Escherichia coli with AMP, Glucose 6-phosphate, and Fructose 1,6-bisphosphate bound

Released:
DOI: 10.2210/pdb2q8m/pdb
PDB entry 2q8m coloured by chain, front view.
PDB entry 2q8m coloured by chain, side view.
PDB entry 2q8m coloured by chain, top view.
Source organism: Shigella boydii
Primary publication:
Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch.
Hines JK, Kruesel CE, Fromm HJ, Honzatko RB
J Biol Chem 282 24697-706 (2007)
PMID: 17567577

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141853 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase class 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 37.16 KDa
Source organism: Shigella boydii
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A993 (Residues: 1-332; Coverage: 100%)
Gene names: JW4191, b4232, fbp, fdp
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand BG6 1 x BG6
Ligand FBP 2 x FBP
Ligand MG 4 x MG
Ligand CL 3 x CL
Ligand AMP 2 x AMP
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P4122
Unit cell:
a: 124.64Å b: 124.64Å c: 132.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.209 0.235
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Positive allosteric modulation of M1 and M4 muscarinic receptors as potential therapeutic treatments for schizophrenia.
Yohn et al. (2018)
1 more

6 mentions without citation

Rational engineering of enzyme allosteric regulation through sequence evolution analysis.
Yang et al. (2012)
5 more