3WHO

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

Summary for 3WHO

• Entry DOI: 10.2210/pdb3who/pdb
• Descriptor: Guanyl-specific ribonuclease Po1 (2 entities in total)
• Functional Keywords: hydrolase
• Biological source: Pleurotus ostreatus (oyster mushroom)
• Total number of polymer chains: 3
• Total formula weight: 32186.13

Authors

Kobayashi, H.,Katsurtani, T.,Hara, Y.,Motoyoshi, N.,Itagaki, T.,Akita, F.,Higashiura, A.,Yamada, Y.,Suzuki, M.,Inokuchi, N. (deposition date: 2013-08-30, release date: 2014-07-02, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.85 Å)