› 2vos

X-ray diffraction
2Å resolution

Mycobacterium tuberculosis Folylpolyglutamate synthase complexed with ADP

Released:
DOI: 10.2210/pdb2vos/pdb
PDB entry 2vos coloured by chain, front view.
PDB entry 2vos coloured by chain, side view.
PDB entry 2vos coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structures of Mycobacterium tuberculosis folylpolyglutamate synthase complexed with ADP and AMPPCP.
Young PG, Smith CA, Metcalf P, Baker EN
Acta Crystallogr D Biol Crystallogr D64 745-53 (2008)
PMID: 18566510

Function and Biology Details

Reaction catalysed: 
ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129425 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tetrahydrofolate synthase Chain: A
Molecule details ›
Chain: A
Length: 487 amino acids
Theoretical weight: 51.2 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O53174 (Residues: 1-487; Coverage: 100%)
Gene names: MT2523, folC
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ADP 1 x ADP
Ligand MG 1 x MG
Ligand CO 4 x CO
Ligand GOL 2 x GOL
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P213
Unit cell:
a: 112.405Å b: 112.405Å c: 112.405Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.157 0.192
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Mycobacterium tuberculosis folate metabolism and the mechanistic basis for para-aminosalicylic acid susceptibility and resistance.
Minato et al. (2015)
3 more

5 mentions without citation

The La and related RNA-binding proteins (LARPs): structures, functions, and evolving perspectives.
Maraia et al. (2017)
4 more