4HAA

Structure of Ribonuclease Binase Glu43Ala/Phe81Ala Mutant

4HAA の概要

• エントリーDOI: 10.2210/pdb4haa/pdb
• 関連するPDBエントリー: 1GOU 1GOV 1GOY
• 分子名称: Ribonuclease (2 entities in total)
• 機能のキーワード: endoribonuclease, hydrolase
• 由来する生物種: Bacillus intermedius
• 細胞内の位置: Secreted: P00649
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 48373.96

構造登録者

Polyakov, K.M.,Trofimov, A.A.,Mitchevich, V.A.,Dorovatovskii, P.V.,Schulga, A.A.,Makarov, A.A.,Tkach, E.N.,Goncharuk, D.A. (登録日: 2012-09-26, 公開日: 2012-10-17, 最終更新日: 2023-09-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)