| Autor: |
Ago, Hideo, Kataoka, Jiro, Tsuge, Hideaki, Habuka, Noriyuki, Inagaki, Eiji, Noma, Masana, Miyano, Masashi |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 10/1/94, Vol. 225 Issue 1, p369-374, 6p |
| Abstrakt: |
We have determined the crystal structure of alpha-pokeweed antiviral protein, a member of ribosome-inactivating proteins, at 0.23 nm resolution, by the molecular-replacement method. The crystals belong to the space group P2[sub1]2[sup1]2 with unit-cell dimensions a = 4.71, b = 11.6[sup3] and c = 4.96 nm, and contain one protein molecule/asymmetric unit based on a crystal volume/unit protein molecular mass of 2.1 x 10([sup-3]nm[sup3]/Da. The crystallographic residual value was reduced to 17.2% (0.6-0.2[sup3]nm resolution) with root-mean-square deviations in bond lengths of 1.9 pm and bond angles of 2.2 %deg;. The C alpha-C alpha distance map shows that alpha-pokeweed antiviral protein is composed of three modules, the N-terminal (Ala1-Leu76), the central (Tyr77-Lys185) and the C-terminal (Tyr186-Thr266) modules. The substrate-binding site is formed as a cleft between the central and C-terminal modules and all the active residues exist on the central module. The electrostatic potential around the substrate-binding site shows that the central and C-terminal module sides of this cleft have a negatively and a positively charged region, respectively. This charge distribution in the protein seems to provide a suitable interaction with the substrate rRNA. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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