› 2c2b

X-ray diffraction
2.6Å resolution

Crystallographic structure of Arabidopsis thaliana Threonine synthase complexed with pyridoxal phosphate and S-adenosylmethionine

Released:
DOI: 10.2210/pdb2c2b/pdb
PDB entry 2c2b coloured by chain, front view.
PDB entry 2c2b coloured by chain, side view.
PDB entry 2c2b coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site.
Mas-Droux C, Biou V, Dumas R
J Biol Chem 281 5188-96 (2006)
PMID: 16319072

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-193418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine synthase 1, chloroplastic Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 486 amino acids
Theoretical weight: 53.39 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9S7B5 (Residues: 41-526; Coverage: 92%)
Gene names: At4g29840, F27B13.80, MTO2, TS1
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 6 x PLP
2 bound ligands:
Ligand SAM 12 x SAM
Ligand TRS 3 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 191.92Å b: 110.846Å c: 152.779Å
α: 90° β: 89.98° γ: 90°
R-values:
R R work R free
0.208 0.206 0.248
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

Interdependence of threonine, methionine and isoleucine metabolism in plants: accumulation and transcriptional regulation under abiotic stress.
Joshi et al. (2010)
7 more

4 mentions without citation

Binding leverage as a molecular basis for allosteric regulation.
Mitternacht et al. (2011)
3 more