3WHO

X-ray-Crystallographic Structure of an RNase Po1 Exhibiting Anti-tumor Activity

3WHO の概要

• エントリーDOI: 10.2210/pdb3who/pdb
• 分子名称: Guanyl-specific ribonuclease Po1 (2 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Pleurotus ostreatus (oyster mushroom)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 32186.13

構造登録者

Kobayashi, H.,Katsurtani, T.,Hara, Y.,Motoyoshi, N.,Itagaki, T.,Akita, F.,Higashiura, A.,Yamada, Y.,Suzuki, M.,Inokuchi, N. (登録日: 2013-08-30, 公開日: 2014-07-02, 最終更新日: 2026-03-04)

主引用文献

Kobayashi, H.,Katsutani, T.,Hara, Y.,Motoyoshi, N.,Itagaki, T.,Akita, F.,Higashiura, A.,Yamada, Y.,Inokuchi, N.,Suzuki, M.
X-ray crystallographic structure of RNase Po1 that exhibits anti-tumor activity.
Biol.Pharm.Bull., 37:968-978, 2014

PubMed Abstract: RNase Po1 is a guanylic acid-specific ribonuclease member of the RNase T1 family from Pleurotus ostreatus. We previously reported that RNase Po1 inhibits the proliferation of human tumor cells, yet RNase T1 and other T1 family RNases are non-toxic. We determined the three-dimensional X-ray structure of RNase Po1 and compared it with that of RNase T1. The catalytic sites are conserved. However, there are three disulfide bonds, one more than in RNase T1. One of the additional disulfide bond is in the catalytic and binding site of RNase Po1, and makes RNase Po1 more stable than RNase T1. A comparison of the electrostatic potential of the molecular surfaces of these two proteins shows that RNase T1 is anionic whereas RNase Po1 is cationic, so RNase Po1 might bind to the plasma membrane electrostatically. We suggest that the structural stability and cationic character of RNase Po1 are critical to the anti-cancer properties of the protein.

PubMed: 24882409
DOI: 10.1248/bpb.b13-00929

実験手法

X-RAY DIFFRACTION (1.85 Å)