1RTA

CRYSTAL STRUCTURE DISPOSITION OF THYMIDYLIC ACID TETRAMER IN COMPLEX WITH RIBONUCLEASE A

Summary for 1RTA

• Entry DOI: 10.2210/pdb1rta/pdb
• Descriptor: DNA (5'-D(*TP*TP*TP*T)-3'), PROTEIN (RIBONUCLEASE A (E.C.3.1.27.5)) (2 entities in total)
• Functional Keywords: protein-dna complex, hydrolase-dna complex, hydrolase/dna
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P61823
• Total number of polymer chains: 2
• Total formula weight: 14880.14

Authors

Birdsall, D.L.,McPherson, A. (deposition date: 1992-08-28, release date: 1993-10-31, Last modification date: 2024-11-13)

Primary citation

Birdsall, D.L.,McPherson, A.
Crystal structure disposition of thymidylic acid tetramer in complex with ribonuclease A.
J.Biol.Chem., 267:22230-22236, 1992

PubMed 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.

PubMed: 1429575

Experimental method

X-RAY DIFFRACTION (2.5 Å)