› 7txb

X-ray diffraction
3.71Å resolution

Structure of the Class II Fructose-1,6-Bisphophatase from Mycobacterium tuberculosis complexed with substrate F1,6BP

Released:
DOI: 10.2210/pdb7txb/pdb
PDB entry 7txb coloured by chain, front view.
PDB entry 7txb coloured by chain, side view.
PDB entry 7txb coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
New structures of Class II Fructose-1,6-Bisphosphatase from Francisella tularensis provide a framework for a novel catalytic mechanism for the entire class.
Selezneva AI, Harding LNM, Gutka HJ, Movahedzadeh F, Abad-Zapatero C
OpenAccess logo PLoS One 18 e0274723 (2023)
PMID: 37352301

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-231848 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase class 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 347 amino acids
Theoretical weight: 36.66 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WN21 (Residues: 35-362; Coverage: 91%)
Gene names: Rv1099c, glpX
Sequence domains: Bacterial fructose-1,6-bisphosphatase, glpX-encoded

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand FBP 2 x FBP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6122
Unit cell:
a: 117.11Å b: 117.11Å c: 325.917Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.213 0.273
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 mention without citation

New structures of Class II Fructose-1,6-Bisphosphatase from Francisella tularensis provide a framework for a novel catalytic mechanism for the entire class.
Selezneva et al. (2023)