Crystal structure of methyl parathion hydrolase from Pseudomonas sp WBC-3
文献类型:期刊论文
作者 | Dong, YJ ; Bartlam, M ; Sun, L ; Zhou, YF ; Zhang, ZP ; Zhang, CG ; Rao, ZH ; Zhang, XE |
刊名 | JOURNAL OF MOLECULAR BIOLOGY
![]() |
出版日期 | 2005 |
卷号 | 353期号:3页码:655-663 |
关键词 | methyl parathion hydrolase crystal structure binuclear metal center metallo-beta-lactamase organophosphate pesticides |
ISSN号 | 0022-2836 |
通讯作者 | Rao, ZH, Chinese Acad Sci, Joint Res Grp Analyt Biotechnol, Inst Biophys, Beijing 100101, Peoples R China |
中文摘要 | Methyl parathion hydrolase (MPH, E.C.3.1.8.1), isolated from the soil-dwelling bacterium Pseudomonas sp. WBC-3, is a Zn(II)-containing enzyme that catalyzes the degradation of the organophosphate pesticide methyl parathion. We have determined the structure of MPH from Pseudomonas sp. WBC-3 to 2.4 angstrom resolution. The enzyme is dimeric and each subunit contains a mixed hybrid binuclear zinc center, in which one of the zinc ions is replaced by cadmium. In both subunits, the more solvent-exposed beta-metal ion is substituted for Cd2+ due to high cadmium concentration in the crystallization condition. Both ions are surrounded by ligands in an octahedral arrangement. The ions are separated by 3.5 angstrom and are coordinated by the amino acid residues His147, His149, Asp151, His152, His234 and His302 and a water molecule. Asp255 and a water molecule serve to bridge the zinc ions together. MPH is homologous with other metallo-beta-lactamases but does not show any similarity to phosphotriesterase that can also catalyze the degradation of methyl parathion with lower rate, despite the lack of sequence homology. Trp179, Phe196 and Phe119 form an aromatic cluster at the entrance of the catalytic center. Replacement of these three amino acids by alanine resulted in a significant increase of Km and loss of catalytic activity, indicating that the aromatic cluster has an important role to facilitate affinity of enzyme to the methyl parathion substrates. (c) 2005 Elsevier Ltd. All rights reserved. |
学科主题 | Biochemistry & Molecular Biology |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000232815900016 |
公开日期 | 2011-09-23 |
源URL | [http://210.72.129.5/handle/321005/55047] ![]() |
专题 | 沈阳应用生态研究所_沈阳应用生态研究所_期刊论文 |
推荐引用方式 GB/T 7714 | Dong, YJ,Bartlam, M,Sun, L,et al. Crystal structure of methyl parathion hydrolase from Pseudomonas sp WBC-3[J]. JOURNAL OF MOLECULAR BIOLOGY,2005,353(3):655-663. |
APA | Dong, YJ.,Bartlam, M.,Sun, L.,Zhou, YF.,Zhang, ZP.,...&Zhang, XE.(2005).Crystal structure of methyl parathion hydrolase from Pseudomonas sp WBC-3.JOURNAL OF MOLECULAR BIOLOGY,353(3),655-663. |
MLA | Dong, YJ,et al."Crystal structure of methyl parathion hydrolase from Pseudomonas sp WBC-3".JOURNAL OF MOLECULAR BIOLOGY 353.3(2005):655-663. |
入库方式: OAI收割
来源:沈阳应用生态研究所
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。