› 1w7k

X-ray diffraction
2.1Å resolution

E.coli FolC in complex with ADP, without folate substrate

Released:
DOI: 10.2210/pdb1w7k/pdb
PDB entry 1w7k coloured by chain, front view.
PDB entry 1w7k coloured by chain, side view.
PDB entry 1w7k coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy.
Mathieu M, Debousker G, Vincent S, Viviani F, Bamas-Jacques N, Mikol V
J Biol Chem 280 18916-22 (2005)
PMID: 15705579

Function and Biology Details

Reactions catalysed: 
ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8-dihydropteroylglutamate
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-140011 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate synthase/folylpolyglutamate synthase Chain: A
Molecule details ›
Chain: A
Length: 422 amino acids
Theoretical weight: 45.5 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08192 (Residues: 1-422; Coverage: 100%)
Gene names: JW2312, b2315, dedC, folC
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ADP 1 x ADP
Ligand SO4 1 x SO4
Ligand MG 2 x MG
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P212121
Unit cell:
a: 66.112Å b: 81.602Å c: 93.673Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.231
Expression system: Escherichia coli

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Citations

6 review citations

Structure, function and dynamics in the mur family of bacterial cell wall ligases.
Smith CA. (2006)
5 more

1 mention without citation

Biological and computational studies provide insights into Caesalphinia digyna Rottler stems.
Emon et al. (2021)