› 2d1f

X-ray diffraction
2.5Å resolution

Structure of Mycobacterium tuberculosis threonine synthase

Released:
DOI: 10.2210/pdb2d1f/pdb
PDB entry 2d1f coloured by chain, front view.
PDB entry 2d1f coloured by chain, side view.
PDB entry 2d1f coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural, biochemical, and in vivo investigations of the threonine synthase from Mycobacterium tuberculosis.
Covarrubias AS, Högbom M, Bergfors T, Carroll P, Mannerstedt K, Oscarson S, Parish T, Jones TA, Mowbray SL
J Mol Biol 381 622-33 (2008)
PMID: 18621388

Function and Biology Details

Reaction catalysed: 
O-phospho-L-homoserine + H(2)O = L-threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161461 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 360 amino acids
Theoretical weight: 37.36 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WG59 (Residues: 1-360; Coverage: 100%)
Gene names: MTCY373.15, Rv1295, thrC
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P61
Unit cell:
a: 55.964Å b: 55.964Å c: 368.378Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.187 0.256
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Controlling reaction specificity in pyridoxal phosphate enzymes.
Toney MD. (2011)
1 more

4 mentions without citation

PRIMO: A Transferable Coarse-grained Force Field for Proteins.
Kar et al. (2013)
3 more