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Crystal structure of the dimeric unswapped form of bovine seminal ribonuclease
Author(s) -
Berisio R,
Sica F,
De Lorenzo C,
Di Fiore A,
Piccoli R,
Zagari A,
Mazzarella L
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01114-1
Subject(s) - ribonuclease , ribonuclease iii , chemistry , rnase p , sexual dimorphism , s tag , crystal structure , resolution (logic) , crystallography , biology , biochemistry , rna , zoology , gene , artificial intelligence , rna interference , computer science
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 Å 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.