› 7a9h

X-ray diffraction
1.85Å resolution

Function and Biology Details

Reaction catalysed: 
Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO(2)
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-161880 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-deoxy-D-xylulose-5-phosphate synthase Chains: AAA, BBB
Molecule details ›
Chains: AAA, BBB
Length: 628 amino acids
Theoretical weight: 66.69 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WNS3 (Residues: 1-189, 235-638; Coverage: 93%)
Gene names: MTCY05A6.03c, Rv2682c, dxs
Sequence domains:

Ligands and Environments


Cofactor: Ligand TPP 2 x TPP
1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Spacegroup: P1
Unit cell:
a: 62.987Å b: 76.1Å c: 79.148Å
α: 108.956° β: 106.53° γ: 107.594°
R-values:
R R work R free
0.151 0.151 0.174
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

1-deoxy-D-xylulose-5-phosphate synthase from Pseudomonas aeruginosa and Klebsiella pneumoniae reveals conformational changes upon cofactor binding.
Hamid et al. (2023)
1 more

1 mention without citation

First crystal structures of 1-deoxy-D-xylulose 5-phosphate synthase (DXPS) from Mycobacterium tuberculosis indicate a distinct mechanism of intermediate stabilization.
Gierse et al. (2022)