› 8g50

X-ray diffraction
1.7Å resolution

E. coli DHFR complex with NADP+ and folate: EF-X excited state model by Laue diffraction (electric field along b axis; 8-fold extrapolation of structure factor differences)

Released:
DOI: 10.2210/pdb8g50/pdb
PDB entry 8g50 coloured by chain, front view.
PDB entry 8g50 coloured by chain, side view.
PDB entry 8g50 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Perturbative diffraction methods resolve a conformational switch that facilitates a two-step enzymatic mechanism.
Greisman JB, Dalton KM, Brookner DE, Klureza MA, Sheehan CJ, Kim IS, Henning RW, Russi S, Hekstra DR
OpenAccess logo Proc Natl Acad Sci U S A 121 e2313192121 (2024)
PMID: 38386706

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142189 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 18.05 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABQ4 (Residues: 1-159; Coverage: 100%)
Gene names: JW0047, b0048, folA, tmrA
Sequence domains: Dihydrofolate reductase

Ligands and Environments


Cofactor: Ligand NAP 2 x NAP
2 bound ligands:
Ligand FOL 2 x FOL
Ligand MN 10 x MN
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P21
Unit cell:
a: 34.286Å b: 45.53Å c: 98.995Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.309 0.306 0.35
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Changes in an enzyme ensemble during catalysis observed by high-resolution XFEL crystallography.
Smith et al. (2024)
3 more

1 mention without citation

Coordinated DNA polymerization by PolĪ³ and the region of LonP1 regulated proteolysis.
Riccio et al. (2024)