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Refinement of the structure of bovine seminal ribonuclease

✍ Scribed by Sante Capasso; Federico Giordano; Carlo A. Mattia; Lelio Mazzarella; Adriana Zagari

Publisher
Wiley (John Wiley & Sons)
Year
1983
Tongue
English
Weight
300 KB
Volume
22
Category
Article
ISSN
0006-3525

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✦ Synopsis

We report here the refinement at 2.5-A resolution of the x-ray crystal structure of bovine seminal rihonuclease, a dimeric covalent enzyme. The protein, which crystallizes with one molecule in the asymmetric unit, consists of two subunits of identical chemical sequences, related by an almost exact binary axis. The tertiary structure of the subunits is similar to that of the pancreatic enzyme, which shows similar catalytic properties. The refinement was carried out using the restrained least-squares procedure both in the reciprocal and real spaces. The assemblage of the subunits in the dimer is described and discussed.

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## Abstract Bovine seminal ribonuclease (BS‐RNase) is a unique member of the pancreatic‐like ribonuclease superfamily. This enzyme exists as two conformational isomers with distinctive biological properties. The structure of the major isomer is characterized by the swapping of the N‐terminal segmen

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