4HAA

Structure of Ribonuclease Binase Glu43Ala/Phe81Ala Mutant

Summary for 4HAA

• Entry DOI: 10.2210/pdb4haa/pdb
• Related: 1GOU 1GOV 1GOY
• Descriptor: Ribonuclease (2 entities in total)
• Functional Keywords: endoribonuclease, hydrolase
• Biological source: Bacillus intermedius
• Cellular location: Secreted: P00649
• Total number of polymer chains: 4
• Total formula weight: 48373.96

Authors

Polyakov, K.M.,Trofimov, A.A.,Mitchevich, V.A.,Dorovatovskii, P.V.,Schulga, A.A.,Makarov, A.A.,Tkach, E.N.,Goncharuk, D.A. (deposition date: 2012-09-26, release date: 2012-10-17, Last modification date: 2023-09-20)

Primary citation

Mitkevich, V.A.,Schulga, A.A.,Trofimov, A.A.,Dorovatovskii, P.V.,Goncharuk, D.A.,Tkach, E.N.,Makarov, A.A.,Polyakov, K.M.
Structure and functional studies of the ribonuclease binase Glu43Ala/Phe81Ala mutant.
Acta Crystallogr.,Sect.D, 69:991-996, 2013

PubMed Abstract: 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.

PubMed: 23695243
DOI: 10.1107/S0907444913004046

Experimental method

X-RAY DIFFRACTION (1.9 Å)