Structure of the scorpion toxin BmBKTtx1 solved from single wavelength anomalous scattering of sulfur
文献类型：期刊论文
| 作者 | Szyk, A; Lu, WY; Xu, CQ; Lubkowski, J |
| 刊名 | JOURNAL OF STRUCTURAL BIOLOGY
 |
| 出版日期 | 2004 |
| 卷号 | 145期号:3页码:289-294 |
| 关键词 | SIRAS from sulfur scorpion toxin BmBKTx1 |
| 通讯作者 | Lubkowski, J (reprint author), NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA.,jacek@ncifcrf.gov |
| 英文摘要 | This report describes the crystal structure of the K+ channel-blocking toxin, BmBKTx1, isolated recently from the venom of the scorpion Buthus martensi Karsch. This is only the second structure of the short-chain K+ channel-blocking toxin from scorpion solved by means of X-ray crystallography. Additionally, reductive dimethylation of folded BmBKTx1 employed to induce its crystallization and solution of the structure based on the anomalous signal from the sulfur atoms make this example quite unique. The monomer of BmBKTx1 is formed by 31 amino acid residues, including 6 cysteines connected in 3 disulfide bridges. Crystals of this toxin belong to the space group P2(1) with two molecules present in the asymmetric unit. The unit cell parameters are a = 21.40 Angstrom, b = 39.70 Angstrom, c = 29.37 Angstrom, and beta = 94.13degrees. Based on the high-quality dataset (anomalous signal) collected to the resolution 1.72 Angstrom using the conventional X-radiation generator (lambda(Cu,Kalpha) = 1.5478 Angstrom), the positions of sulfur atoms contributed by 12 cysteine residues have been identified, and subsequent improvement of the experimental phases have allowed structure solution. The final model was refined to the crystallographic R-factor of 0.166. The methyl groups on several lysine residues could be easily modeled into the electron density. Published by Elsevier Inc. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| 关键词[WOS] | PROTEIN CRYSTALLOGRAPHY ; LYSINE RESIDUES ; SODIUM-CHANNELS ; REFINEMENT ; RESOLUTION ; MOLSCRIPT ; INSIGHTS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000189018600012 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2061]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Szyk, A,Lu, WY,Xu, CQ,et al. Structure of the scorpion toxin BmBKTtx1 solved from single wavelength anomalous scattering of sulfur[J]. JOURNAL OF STRUCTURAL BIOLOGY,2004,145(3):289-294. |
| APA | Szyk, A,Lu, WY,Xu, CQ,&Lubkowski, J.(2004).Structure of the scorpion toxin BmBKTtx1 solved from single wavelength anomalous scattering of sulfur.JOURNAL OF STRUCTURAL BIOLOGY,145(3),289-294. |
| MLA | Szyk, A,et al."Structure of the scorpion toxin BmBKTtx1 solved from single wavelength anomalous scattering of sulfur".JOURNAL OF STRUCTURAL BIOLOGY 145.3(2004):289-294. |
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