3U01

Crystal structure of onconase double mutant C30A/C75A at 1.12 A resolution

3U01 の概要

• エントリーDOI: 10.2210/pdb3u01/pdb
• 関連するPDBエントリー: 1ONC 1U00 3HG6 3PHN
• 分子名称: Protein P-30, SULFATE ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta protein, ranpirnase, endonuclease, nuclease, hydrolase, antitumor protein
• 由来する生物種: Rana pipiens (Northern leopard frog)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12128.75

構造登録者

Kurpiewska, K.,Torrent, G.,Ribo, M.,Vilanova, M.,Loch, J.,Lewinski, K. (登録日: 2011-09-28, 公開日: 2011-12-21, 最終更新日: 2024-11-20)

主引用文献

Kurpiewska, K.,Torrent, G.,Ribo, M.,Loch, J.I.,Vilanova, M.,Lewinski, K.
Investigating the effects of double mutation C30A/C75A on onconase structure: Studies at atomic resolution.
Biopolymers, 101:454-460, 2014

PubMed Abstract: The structure of onconase C30A/C75A double mutant has been determined at 1.12Å resolution. The structure has high structural homology to other onconase structures. The changes being results of mutation are relatively small, distributed asymmetrically around the two mutated positions, and they are observed not only in the mutation region but expanded to entire molecule. Different conformation of Lys31 side chain that influences the hydrogen bonding network around catalytic triad is probably responsible for lower catalytic efficiency of double mutant. The decrease in thermal stability observed for the onconase variant might be explained by a less dense packing as manifested by the increase of the molecular volume and the solvent accessible surface area.

PubMed: 23996687
DOI: 10.1002/bip.22403

実験手法

X-RAY DIFFRACTION (1.12 Å)