Crystal Structure of a Four-Layer Aggregate of Engineered TMV CP Implies the Importance of Terminal Residues for Oligomer Assembly
文献类型：期刊论文
| 作者 | Li, Xiangyang2; Song, Baoan2; Chen, Xi2; Wang, Zhenchao2; Zeng, Mengjiao3; Yu, Dandan2; Hu, Deyu2; Chen, Zhuo2; Jin, Linhong2; Yang, Song2 |
| 刊名 | PLOS ONE
 |
| 出版日期 | 2013-11-04 |
| 卷号 | 8期号:11 |
| ISSN号 | 1932-6203 |
| DOI | 10.1371/journal.pone.0077717 |
| 文献子类 | Article |
| 英文摘要 | Background: Crystal structures of the tobacco mosaic virus (TMV) coat protein (CP) in its helical and disk conformations have previously been determined at the atomic level. For the helical structure, interactions of proteins and nucleic acids in the main chains were clearly observed; however, the conformation of residues at the C-terminus was flexible and disordered. For the four-layer aggregate disk structure, interactions of the main chain residues could only be observed through water-mediated hydrogen bonding with protein residues. In this study, the effects of the C-terminal peptides on the interactions of TMV CP were investigated by crystal structure determination. Methodology/Principal Findings: The crystal structure of a genetically engineered TMV CP was resolved at 3.06 angstrom. For the genetically engineered TMV CP, a six-histidine (His) tag was introduced at the N-terminus, and the C-terminal residues 155 to 158 were truncated (N-His-TMV CP19). Overall, N-His-TMV CP19 protein self-assembled into the four-layer aggregate form. The conformations of residues Gln36, Thr59, Asp115 and Arg134 were carefully analyzed in the high radius and low radius regions of N-His-TMV CP19, which were found to be significantly different from those observed previously for the helical and four-layer aggregate forms. In addition, the aggregation of the N-His-TMV CP19 layers was found to primarily be mediated through direct hydrogen-bonding. Notably, this engineered protein also can package RNA effectively and assemble into an infectious virus particle. Conclusion: The terminal sequence of amino acids influences the conformation and interactions of the four-layer aggregate. Direct protein-protein interactions are observed in the major overlap region when residues Gly155 to Thr158 at the C-terminus are truncated. This engineered TMV CP is reassembled by direct protein-protein interaction and maintains the normal function of the four-layer aggregate of TMV CP in the presence of RNA. |
| WOS关键词 | TOBACCO-MOSAIC-VIRUS ; RAY FIBER DIFFRACTION ; COAT PROTEIN ; ELECTRON-MICROSCOPY ; MAXIMUM-LIKELIHOOD ; PACKAGING MOTOR ; RESOLUTION ; RNA ; MECHANISM ; DISK |
| 资助项目 | National Basic Research Program of China[2010CB126105] ; Key Technologies RD Program[2011BAE06B05-6] ; National Natural Science Foundation of China[21132003] |
| WOS研究方向 | Science & Technology - Other Topics |
| 语种 | 英语 |
| WOS记录号 | WOS:000326503400014 |
| 出版者 | PUBLIC LIBRARY SCIENCE |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/277382]  |
| 专题 | 药理学第三研究室 |
| 通讯作者 | Song, Baoan |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 200031, Peoples R China 2.Guizhou Univ, State Key Lab Breeding Base Green Pesticide & Agr, Key Lab Green Pesticide & Agr Bioengn, Minist Educ, Guiyang 550003, Peoples R China; 3.S China Univ Technol, Sch Chem & Chem Engn, Guangzhou, Guangdong, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Li, Xiangyang,Song, Baoan,Chen, Xi,et al. Crystal Structure of a Four-Layer Aggregate of Engineered TMV CP Implies the Importance of Terminal Residues for Oligomer Assembly[J]. PLOS ONE,2013,8(11). |
| APA | Li, Xiangyang.,Song, Baoan.,Chen, Xi.,Wang, Zhenchao.,Zeng, Mengjiao.,...&Chen, Baoen.(2013).Crystal Structure of a Four-Layer Aggregate of Engineered TMV CP Implies the Importance of Terminal Residues for Oligomer Assembly.PLOS ONE,8(11). |
| MLA | Li, Xiangyang,et al."Crystal Structure of a Four-Layer Aggregate of Engineered TMV CP Implies the Importance of Terminal Residues for Oligomer Assembly".PLOS ONE 8.11(2013). |
入库方式： OAI收割
来源：上海药物研究所
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