| Autor: |
Zhang X; California NanoSystems Institute, University of California, Los Angeles, Los Angeles, United States., Guo H, Jin L, Czornyj E, Hodes A, Hui WH, Nieh AW, Miller JF, Zhou ZH |
| Jazyk: |
angličtina |
| Zdroj: |
ELife [Elife] 2013 Dec 17; Vol. 2, pp. e01299. Date of Electronic Publication: 2013 Dec 17. |
| DOI: |
10.7554/eLife.01299 |
| Abstrakt: |
Bacteriophage BPP-1 infects and kills Bordetella species that cause whooping cough. Its diversity-generating retroelement (DGR) provides a naturally occurring phage-display system, but engineering efforts are hampered without atomic structures. Here, we report a cryo electron microscopy structure of the BPP-1 head at 3.5 Å resolution. Our atomic model shows two of the three protein folds representing major viral lineages: jellyroll for its cement protein (CP) and HK97-like ('Johnson') for its major capsid protein (MCP). Strikingly, the fold topology of MCP is permuted non-circularly from the Johnson fold topology previously seen in viral and cellular proteins. We illustrate that the new topology is likely the only feasible alternative of the old topology. β-sheet augmentation and electrostatic interactions contribute to the formation of non-covalent chainmail in BPP-1, unlike covalent inter-protein linkages of the HK97 chainmail. Despite these complex interactions, the termini of both CP and MCP are ideally positioned for DGR-based phage-display engineering. DOI: http://dx.doi.org/10.7554/eLife.01299.001. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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