Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme
文献类型：期刊论文
| 作者 | Li, J; Xia, ZX; Ding, JP |
| 刊名 | PROTEIN SCIENCE
 |
| 出版日期 | 2005 |
| 卷号 | 14期号:9页码:2361-2369 |
| 关键词 | glutathione transferase crystal structure active site glutathione sulfinate thioredoxin-like domain glutathione peroxidase |
| 通讯作者 | Xia, ZX (reprint author), Chinese Acad Sci, Shanghai Inst Organ Chem, State Key lab Bioorgan & Nat Prod Chem, 354 Fenglin Rd, Shanghai 200032, Peoples R China.,xiazx@mail.sioc.ac.cn ; jpding@sibs.ac.cn |
| 英文摘要 | Glutathione transferases (GSTs) are a superfamily of enzymes that play a vital functional role in the cellular detoxification process. They catalyze the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a wide range of hydrophobic substrates, leading to an easier removal of the latter from the cells. The K class is the least studied one among various classes within the superfamily. We report here the expression, purification, and crystal structure of human kappa class GST (hGSTK), which has been determined by the multiple-isomorphous replacement method and refined to 1.93 angstrom resolution. The overall structure of hGSTK is similar to the recently reported structure of K class GST from rat mitochondrion. Each subunit of the dimeric hGSTK contains a thioredoxin (TRX)-like domain and a helical domain. A molecule of glutathione sulfinate, an oxidized product of GSH, is found to bind at the G site of each monomer. One oxygen atom of the sulfino group of GSF forms a hydrogen bond with the hydroxyl group of the catalytic residue Ser16. The TRX-like domain of hGSTK shares 19% sequence identity and structure similarity with human theta class GST, suggesting that the kappa class of GST is more closely related to the theta class enzyme within the GST superfamily. The structure of the TRX-like domain of hGSTK is also similar to that of glutathione peroxidase (GPx), implying an evolutionary relationship between GST and GPx. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | S-TRANSFERASE ; CRYSTAL-STRUCTURE ; 3-DIMENSIONAL STRUCTURE ; ANGSTROM RESOLUTION ; PEROXIDASE ; IDENTIFICATION ; GENE ; SITE ; SELENOCYSTEINE ; MECHANISM |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000231607500018 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1954]  |
| 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 | Li, J,Xia, ZX,Ding, JP. Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme[J]. PROTEIN SCIENCE,2005,14(9):2361-2369. |
| APA | Li, J,Xia, ZX,&Ding, JP.(2005).Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme.PROTEIN SCIENCE,14(9),2361-2369. |
| MLA | Li, J,et al."Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme".PROTEIN SCIENCE 14.9(2005):2361-2369. |
入库方式： OAI收割
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。