Structural highlights
Function
[RNS_BOVIN] This enzyme hydrolyzes both single- and double-stranded RNA.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bovine seminal ribonuclease is a unique case of protein dimorphism, since it exists in two dimeric forms, with different biological and kinetic behavior, which interconvert into one another through three-dimensional swapping. Here we report the crystal structure, at 2.2 A resolution, of the unswapped form of bovine seminal ribonuclease. Besides completing the structural definition of bovine seminal ribonuclease conformational dimorphism, this study provides the structural basis to explain the dependence of the enzyme cooperative effects on its swapping state.
Crystal structure of the dimeric unswapped form of bovine seminal ribonuclease.,Berisio R, Sica F, De Lorenzo C, Di Fiore A, Piccoli R, Zagari A, Mazzarella L FEBS Lett. 2003 Nov 6;554(1-2):105-10. PMID:14596923[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Berisio R, Sica F, De Lorenzo C, Di Fiore A, Piccoli R, Zagari A, Mazzarella L. Crystal structure of the dimeric unswapped form of bovine seminal ribonuclease. FEBS Lett. 2003 Nov 6;554(1-2):105-10. PMID:14596923
