| Autor: |
Mitkevich VA; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, Moscow 119991, Russian Federation., Schulga AA, Trofimov AA, Dorovatovskii PV, Goncharuk DA, Tkach EN, Makarov AA, Polyakov KM |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2013 Jun; Vol. 69 (Pt 6), pp. 991-6. Date of Electronic Publication: 2013 May 11. |
| DOI: |
10.1107/S0907444913004046 |
| Abstrakt: |
Ribonuclease from Bacillus intermedius (binase) is a small basic protein with antitumour activity. The three-dimensional structure of the binase mutant form Glu43Ala/Phe81Ala was determined at 1.98 Å resolution and its functional properties, such as the kinetic parameters characterizing the hydrolysis of polyinosinic acid and cytotoxicity towards Kasumi-1 cells, were investigated. In all crystal structures of binase studied previously the characteristic dimer is present, with the active site of one subunit being blocked owing to interactions within the dimer. In contrast to this, the new mutant form is not dimeric in the crystal. The catalytic efficiency of the mutant form is increased 1.7-fold and its cytotoxic properties are enhanced compared with the wild-type enzyme. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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