› 4oof

X-ray diffraction
2.3Å resolution

M. tuberculosis 1-deoxy-d-xylulose-5-phosphate reductoisomerase W203F mutant bound to fosmidomycin and NADPH

Released:
DOI: 10.2210/pdb4oof/pdb
PDB entry 4oof coloured by chain, front view.
PDB entry 4oof coloured by chain, side view.
PDB entry 4oof coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Alteration of the flexible loop in 1-deoxy-D-xylulose-5-phosphate reductoisomerase boosts enthalpy-driven inhibition by fosmidomycin.
Kholodar SA, Tombline G, Liu J, Tan Z, Allen CL, Gulick AM, Murkin AS
OpenAccess logo Biochemistry 53 3423-31 (2014)
PMID: 24825256

Function and Biology Details

Reaction catalysed: 
2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161879 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-deoxy-D-xylulose 5-phosphate reductoisomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 403 amino acids
Theoretical weight: 42.27 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WNS1 (Residues: 1-389; Coverage: 94%)
Gene names: MTCY274.01c, Rv2870c, dxr
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
2 bound ligands:
Ligand MN 2 x MN
Ligand FOM 2 x FOM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P43212
Unit cell:
a: 107.912Å b: 107.912Å c: 136.438Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.159 0.212
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mechanism and inhibition of 1-deoxy-D-xylulose-5-phosphate reductoisomerase.
Murkin et al. (2014)
5 other articles

1 mention without citation

Alteration of the flexible loop in 1-deoxy-D-xylulose-5-phosphate reductoisomerase boosts enthalpy-driven inhibition by fosmidomycin.
Kholodar et al. (2014)