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ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 1994/10 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | X-RAY STRUCTURE OF A POKEWEED ANTIVIRAL PROTEIN, CODED BY A NEW GENOMIC CLONE, AT 0.23 NM RESOLUTION - A MODEL STRUCTURE PROVIDES A SUITABLE ELECTROSTATIC-FIELD FOR SUBSTRATE-BINDING |
| 執筆形態 | その他 |
| 掲載誌名 | EUROPEAN JOURNAL OF BIOCHEMISTRY |
| 出版社・発行元 | SPRINGER VERLAG |
| 巻・号・頁 | 225(1),pp.369-374 |
| 著者・共著者 | H AGO,J KATAOKA,H TSUGE,N HABUKA,E INAGAKI,M NOMA,M MIYANO |
| 概要 | We have determined the crystal structure of a-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(1)2(1)2 with unit-cell dimensions a = 4.71, b = 11.63 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(-3)nm(3)/Da. The crystallographic residual value was reduced to 17.2% (0.6-0.23 nm resolution) with root-mean-square deviations in bond lengths of 1.9 pm and bond angles of 2.2 degrees.
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. |
| DOI | 10.1111/j.1432-1033.1994.00369.x |
| ISSN | 0014-2956 |