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
The interactions between the cytotoxic paddlewheel dirhodium complex [Rh2(mu-O2CCH3)4] and the model protein bovine pancreatic ribonuclease (RNase A) were investigated by high-resolution mass spectrometry and X-ray crystallography. The results indicate that [Rh2(mu-O2CCH3)4] extensively reacts with RNase A. The metal compound binds the protein via coordination of the imidazole ring of a His side chain to one of its axial sites, while the dirhodium center and the acetato ligands remain unmodified. Data provide valuable information for the design of artificial dirhodium-containing metalloenzymes.
Protein interactions of dirhodium tetraacetate: a structural study.,Ferraro G, Pratesi A, Messori L, Merlino A Dalton Trans. 2020 Feb 5. doi: 10.1039/c9dt04819g. PMID:32022076[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
- ↑ Ferraro G, Pratesi A, Messori L, Merlino A. Protein interactions of dirhodium tetraacetate: a structural study. Dalton Trans. 2020 Feb 5. doi: 10.1039/c9dt04819g. PMID:32022076 doi:http://dx.doi.org/10.1039/c9dt04819g
