Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein
文献类型：期刊论文
| 作者 | Zhang, Liang; Liu, Weizhi; Xiao, Jianfeng; Hu, Tiancen; Chen, Jing ; Chen, Kaixian; Jiang, Hualiang; Shen, Xu
|
| 刊名 | PROTEIN SCIENCE
 |
| 出版日期 | 2007-06 |
| 卷号 | 16期号:6页码:1184-1192 |
| 关键词 | Helicobacter pylori Manoyl-CoA acyl carrier protein transacylase (MCAT) acyl carrier protein (ACP) fatty acid biosynthesis crystal structure |
| ISSN号 | 0961-8368 |
| DOI | 10.1110/ps.072757307 |
| 文献子类 | Article |
| 英文摘要 | Malonyl-CoA: acyl carrier protein transacylase (MCAT) is a critical enzyme responsible for the transfer of the malonyl moiety to holo-acyl carrier protein (ACP) forming the malonyl-ACP intermediates in the initiation step of type II fatty acid synthesis (FAS II) in bacteria. MCAT has been considered as an attractive drug target in the discovery of antibacterial agents. In this study, the crystal structure of MCAT from Helicobacter pylori (Hp) at 2.5 angstrom resolution is reported, and the interaction of HpMCAT with HpACP is extensively investigated by using computational docking, GST-pull-down, and surface plasmon resonance (SPR) technology-based assays. The crystal structure results reveal that HpMCAT has a compact folding composed of a large subdomain with a similar core as in alpha/beta hydrolases, and a similar ferredoxin-like small subdomain as in acylphosphatases. The docking result suggests two positively charged areas near the entrance of the active site of HpMCAT as the ACP-binding region. Binding assay research shows that HpMCAT demonstrates a moderately binding ability against HpACP. The solved 3D structure of HpMCAT is expected to supply useful information for the structure-based discovery of novel inhibitors against MCAT, and the quantitative study of HpMCAT interaction with HpACP is hoped to give helpful hints in the understanding of the detailed catalytic mechanisms for HpMCAT. |
| WOS关键词 | FATTY-ACID BIOSYNTHESIS ; ANTIBACTERIAL DRUG DISCOVERY ; ACP DOCKING SITE ; ESCHERICHIA-COLI ; NUCLEOCAPSID PROTEIN ; SYNTHASE ; PURIFICATION ; DEHYDRATASE ; CORONAVIRUS ; REFINEMENT |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000246727100017 |
| 出版者 | WILEY-BLACKWELL |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/273252]  |
| 专题 | 药物发现与设计中心 中科院受体结构与功能重点实验室 新药研究国家重点实验室 药理学第三研究室 |
| 通讯作者 | Jiang, Hualiang |
| 作者单位 | Chinese Acad Sci, Shanghai Inst Mat Med, Drug Discovery & Design Ctr, State Key Lab Drug Res, Shanghai 201203, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, Liang,Liu, Weizhi,Xiao, Jianfeng,et al. Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein[J]. PROTEIN SCIENCE,2007,16(6):1184-1192. |
| APA | Zhang, Liang.,Liu, Weizhi.,Xiao, Jianfeng.,Hu, Tiancen.,Chen, Jing.,...&Shen, Xu.(2007).Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein.PROTEIN SCIENCE,16(6),1184-1192. |
| MLA | Zhang, Liang,et al."Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein".PROTEIN SCIENCE 16.6(2007):1184-1192. |
入库方式： OAI收割
来源：上海药物研究所
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