› 2oip

X-ray diffraction
2.8Å resolution

Crystal Structure of the S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis

Released:
DOI: 10.2210/pdb2oip/pdb
PDB entry 2oip coloured by chain, front view.
PDB entry 2oip coloured by chain, side view.
PDB entry 2oip coloured by chain, top view.
Source organism: Cryptosporidium hominis
Primary publication:
Nonconserved residues Ala287 and Ser290 of the Cryptosporidium hominis thymidylate synthase domain facilitate its rapid rate of catalysis.
Doan LT, Martucci WE, Vargo MA, Atreya CE, Anderson KS
Biochemistry 46 8379-91 (2007)
PMID: 17580969

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163107 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chain A, crystal structure of Dhfr Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 519 amino acids
Theoretical weight: 60.01 KDa
Source organism: Cryptosporidium hominis
Expression system: Escherichia coli BL21(DE3)
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand UMP 5 x UMP
Ligand CB3 5 x CB3
Ligand MTX 5 x MTX
Ligand NDP 5 x NDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: C2
Unit cell:
a: 215.026Å b: 116.204Å c: 216.601Å
α: 90° β: 94.27° γ: 90°
R-values:
R R work R free
0.222 0.222 0.259
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Cryptosporidium: genomic and biochemical features.
Rider et al. (2010)
11 other articles

2 mentions without citation

Exploring novel strategies for AIDS protozoal pathogens: α-helix mimetics targeting a key allosteric protein-protein interaction in C. hominis TS-DHFR.
Martucci et al. (2013)
1 more