Summary information and primary citation
- PDB-id
-
1rta;
DSSR-derived features in text and
JSON formats
- Class
- hydrolase-DNA
- Method
- X-ray (2.5 Å)
- Summary
- Crystal structure disposition of thymidylic acid
tetramer in complex with ribonuclease a
- Reference
-
Birdsall DL, McPherson A (1992): "Crystal
structure disposition of thymidylic acid tetramer in
complex with ribonuclease A." J.Biol.Chem.,
267, 22230-22236.
- Abstract
- The crystal structure of ribonuclease A with bound
thymidylic acid tetramer is reported at 2.5-A resolution.
The diffusion of the tetramer into native orthorhombic
crystals of the ribonuclease allows for the formation of a
structurally stable complex where the single-stranded
nucleic acid enters and leaves the enzyme's catalytic
region in a persistent 5'-3' direction. The binding of the
tetramer to the enzyme's surface is facilitated and
mediated by electrostatic interactions between basic
protein residues and nucleotide phosphates. Two pyrimidine
nucleotides are bound to the enzyme's active site in a
manner similar to that observed for other complexes between
ribonuclease A and nucleic acid oligomers.