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  • Title: Preliminary crystal structure analysis of a microbial, guanine-specific ribonuclease St at 2.5 A resolution.
    Author: Yamamoto Y, Iwahashi K, Nakamura KT, Iitaka Y, Mitsui Y.
    Journal: Nucleic Acids Symp Ser; 1981; (10):227-31. PubMed ID: 6796945.
    Abstract:
    The three-dimensional structure of Ribonuclease St (RNase St), the extracellular ribonuclease from Streptomyces erythreus, has been deduced based on a preliminary electron density map at 2.5 A resolution. RNase St has a substrate specificity similar to ribonuclease T1 which catalyzes the splitting of the phosphodiester bond of guanylic acid. Crystals grown as diamond plates have space group C2 with unit cell parameters a=88.4, b=33.0, c=69.0 A, beta = 98.4 degrees having two enzyme molecules per asymmetric unit. Phases were obtained by use of KAu(CN)4, phenylmercuric acetate and UO2 (CH3COO)2. The overall dimensions of the molecule are 40 X 30 X 25 A. The most prominent secondary structural features are two turns of alpha-helix and a three strand stretch of antiparallel beta-sheet. The alpha-carbon backbone of RNase St seems to have no apparent correlation with that of ribonuclease A.
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