› 2jcv

X-ray diffraction
2.2Å resolution

X-ray structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, DXR, Rv2870c, from Mycobacterium tuberculosis, in complex with fosmidomycin and NADPH

Released:
DOI: 10.2210/pdb2jcv/pdb
PDB entry 2jcv coloured by chain, front view.
PDB entry 2jcv coloured by chain, side view.
PDB entry 2jcv coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structures of Mycobacterium tuberculosis 1-deoxy-D-xylulose-5-phosphate reductoisomerase provide new insights into catalysis.
Henriksson LM, Unge T, Carlsson J, Aqvist J, Mowbray SL, Jones TA
J Biol Chem 282 19905-16 (2007)
PMID: 17491006

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: 398 amino acids
Theoretical weight: 41.7 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
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 FOM 1 x FOM
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 67.348Å b: 65.476Å c: 86.086Å
α: 90° β: 101.56° γ: 90°
R-values:
R R work R free
0.163 0.16 0.209
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Mechanistic aspects of carotenoid biosynthesis.
Moise et al. (2014)
12 more

1 mention without citation

Inhibition of 1-deoxy-D-xylulose-5-phosphate reductoisomerase by lipophilic phosphonates: SAR, QSAR, and crystallographic studies.
Deng et al. (2011)