› 1x92

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA PHOSPHOHEPTOSE ISOMERASE IN COMPLEX WITH REACTION PRODUCT D-GLYCERO-D-MANNOPYRANOSE-7-PHOSPHATE

Released:
DOI: 10.2210/pdb1x92/pdb
PDB entry 1x92 coloured by chain, front view.
PDB entry 1x92 coloured by chain, side view.
PDB entry 1x92 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191034 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoheptose isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 199 amino acids
Theoretical weight: 21.63 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HVZ0 (Residues: 1-197; Coverage: 100%)
Gene names: PA4425, gmhA
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

1 bound ligand:
Ligand M7P 2 x M7P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P6522
Unit cell:
a: 126.338Å b: 126.338Å c: 113.24Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.176 0.221
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

8 mentions without citation

The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes.
Keyamura et al. (2007)
7 more