› 2i22

X-ray diffraction
2.8Å resolution

Crystal structure of Escherichia coli phosphoheptose isomerase in complex with reaction substrate sedoheptulose 7-phosphate

Released:
DOI: 10.2210/pdb2i22/pdb
PDB entry 2i22 coloured by chain, front view.
PDB entry 2i22 coloured by chain, side view.
PDB entry 2i22 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants.
Taylor PL, Blakely KM, de Leon GP, Walker JR, McArthur F, Evdokimova E, Zhang K, Valvano MA, Wright GD, Junop MS
J Biol Chem 283 2835-45 (2008)
PMID: 18056714

Function and Biology Details

Reaction catalysed: 
D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoheptose isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 212 amino acids
Theoretical weight: 23.01 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63224 (Residues: 1-192; Coverage: 100%)
Gene names: JW0212, b0222, gmhA, lpcA, tfrA, yafI
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

1 bound ligand:
Ligand I22 1 x I22
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 73.045Å b: 76.54Å c: 78.316Å
α: 90° β: 106.13° γ: 90°
R-values:
R R work R free
0.207 0.203 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The return of metabolism: biochemistry and physiology of the pentose phosphate pathway.
Stincone et al. (2015)
3 more

5 mentions without citation

Structural model for phenylalkylamine binding to L-type calcium channels.
Cheng et al. (2009)
4 more