› 1otp

X-ray diffraction
2.8Å resolution

STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE

Released:
DOI: 10.2210/pdb1otp/pdb
PDB entry 1otp coloured by chain, front view.
PDB entry 1otp coloured by chain, side view.
PDB entry 1otp coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase.
Pugmire MJ, Cook WJ, Jasanoff A, Walter MR, Ealick SE
J Mol Biol 281 285-99 (1998)
PMID: 9698549

Function and Biology Details

Reaction catalysed: 
Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139679 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 78Å b: 97.4Å c: 137.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.248

Quick links

Citations

5 review citations

Structural analyses reveal two distinct families of nucleoside phosphorylases.
Pugmire et al. (2002)
4 more

1 mention without citation

Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.
Mayans et al. (2002)