› 1tk9

X-ray diffraction
2.1Å resolution

Crystal Structure of Phosphoheptose isomerase 1

Released:
DOI: 10.2210/pdb1tk9/pdb
PDB entry 1tk9 coloured by chain, front view.
PDB entry 1tk9 coloured by chain, side view.
PDB entry 1tk9 coloured by chain, top view.
Source organism: Campylobacter jejuni
Primary publication:
Crystal structures of two putative phosphoheptose isomerases.
Seetharaman J, Rajashankar KR, Solorzano V, Kniewel R, Lima CD, Bonanno JB, Burley SK, Swaminathan S
Proteins 63 1092-6 (2006)
PMID: 16477602

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-192926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoheptose isomerase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 188 amino acids
Theoretical weight: 20.55 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9PNE6 (Residues: 2-186; Coverage: 100%)
Gene names: Cj1149c, gmhA, gmhA1
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A
Spacegroup: P212121
Unit cell:
a: 52.657Å b: 123.289Å c: 127.804Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.211
Expression system: Escherichia coli

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Citations

4 citation in other articles

Structural similarity between the DnaA-binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli.
Natrajan et al. (2007)
3 more

6 mentions without citation

Functional and structural studies on the Neisseria gonorrhoeae GmhA, the first enzyme in the glycero-manno-heptose biosynthesis pathways, demonstrate a critical role in lipooligosaccharide synthesis and gonococcal viability.
Wierzbicki et al. (2017)
5 more