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| Single molecule atomic force microscopy of aerolysin pore complexes reveals unexpected star-shaped topography | |
| He, JF; Wang, JB; Hu, J; Sun, JL; Czajkowsky, DM; Shao, ZF; Sun, JL (reprint author), Shanghai Jiao Tong Univ, Syst Biomed, 800 Dongchuan Rd, Shanghai, Peoples R China.; Czajkowsky, DM (reprint author), Shanghai Jiao Tong Univ, Sch Biomed Engn, 800 Dongchuan Rd, Shanghai, Peoples R China. | |
| 2016 | |
| Source Publication | JOURNAL OF MOLECULAR RECOGNITION
 |
| ISSN | 0952-3499 |
| Volume | 29Issue:4Pages:174—181 |
| Subtype | 期刊文献 |
| Abstract | Aerolysin is the paradigmatic member of a large family of toxins that convert from a water-soluble monomer/dimer into a membrane-spanning oligomeric pore. While there is x-ray crystallographic data of its water-soluble conformation, the most recent structural model of the membrane-inserted pore is based primarily on data of water-soluble tetradecamers of mutant protein, together with computational modeling ultimately performed in vacuum. Here we examine this pore model with atomic force microscopy (AFM) of membrane-associated wild-type complexes and all-atom molecular dynamics (MD) simulations in water. In striking contrast to a disc-shaped cap region predicted by the present model, the AFM images reveal a star-shaped complex, with a central ring surrounded by seven radial projections. Further, the MD simulations suggest that the locations of the receptor-binding (D1) domains in the present model are not correct. However, a modified model in which the D1 domains, rather than localized at fixed positions, adopt a wide range of configurations through fluctuations of an intervening linker is compatible with existing data. Thus our work not only demonstrates the importance of directly resolving such complexes in their native environment but also points to a dynamic receptor binding region, which may be critical for toxin assembly on the cell surface. Copyright (c) 2015 John Wiley & Sons, Ltd. |
| Keyword | Forming Toxin Aerolysin Biological Applications Receptor-binding Membrane-channel Alpha-toxin Dynamics Surface Afm Heptamerization Proaerolysin |
| DOI | 10.1002/jmr.2517 |
| Indexed By | SCI |
| Language | 英语 |
| WOS ID | WOS:000372642700006 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.sinap.ac.cn/handle/331007/25833 |
| Collection | 中科院上海应用物理研究所2011-2020年 |
| Corresponding Author | Sun, JL (reprint author), Shanghai Jiao Tong Univ, Syst Biomed, 800 Dongchuan Rd, Shanghai, Peoples R China.; Czajkowsky, DM (reprint author), Shanghai Jiao Tong Univ, Sch Biomed Engn, 800 Dongchuan Rd, Shanghai, Peoples R China. |
| Recommended Citation GB/T 7714 | He, JF,Wang, JB,Hu, J,et al. Single molecule atomic force microscopy of aerolysin pore complexes reveals unexpected star-shaped topography[J]. JOURNAL OF MOLECULAR RECOGNITION,2016,29(4):174—181. |
| APA | He, JF.,Wang, JB.,Hu, J.,Sun, JL.,Czajkowsky, DM.,...&Czajkowsky, DM .(2016).Single molecule atomic force microscopy of aerolysin pore complexes reveals unexpected star-shaped topography.JOURNAL OF MOLECULAR RECOGNITION,29(4),174—181. |
| MLA | He, JF,et al."Single molecule atomic force microscopy of aerolysin pore complexes reveals unexpected star-shaped topography".JOURNAL OF MOLECULAR RECOGNITION 29.4(2016):174—181. |
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| Single molecule atom（4120KB） | 期刊论文 | 作者接受稿 | 开放获取 | CC BY-NC-SA | View Download | |
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