Structural highlights
Function
RNAS1_BOVIN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1]
Publication Abstract from PubMed
A Raman-assisted crystallographic study on the adduct between AziRu, a Ru(III) complex with high antiproliferative activity, and RNase A is presented. The protein structure is not perturbed significantly by the Ru label. The metal coordinates to ND atoms of His105 or of His119 imidazole rings, losing all of its original ligands but retaining octahedral, although distorted, coordination geometry. The AziRu binding inactivates the enzyme, suggesting that its antitumor action can be exerted by a mechanism of competitive inhibition.
Investigating the ruthenium metalation of proteins: X-ray structure and Raman microspectroscopy of the complex between RNase A and AziRu.,Vergara A, Russo Krauss I, Montesarchio D, Paduano L, Merlino A Inorg Chem. 2013 Oct 7;52(19):10714-6. doi: 10.1021/ic401494v. Epub 2013 Sep 16. PMID:24093479[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73. PMID:7479688
- ↑ Vergara A, Russo Krauss I, Montesarchio D, Paduano L, Merlino A. Investigating the ruthenium metalation of proteins: X-ray structure and Raman microspectroscopy of the complex between RNase A and AziRu. Inorg Chem. 2013 Oct 7;52(19):10714-6. doi: 10.1021/ic401494v. Epub 2013 Sep 16. PMID:24093479 doi:http://dx.doi.org/10.1021/ic401494v
