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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 \u00c5 resolution. Our atomic model shows two of the three protein folds representing major viral lineages: jellyroll for its cement protein (CP) and HK97-like (\u2018Johnson\u2019) 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. \u03b2-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.<\/jats:p>","DOI":"10.7554\/elife.01299","type":"journal-article","created":{"date-parts":[[2013,12,17]],"date-time":"2013-12-17T12:45:42Z","timestamp":1387284342000},"source":"Crossref","is-referenced-by-count":54,"title":["A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 \u00c5 resolution"],"prefix":"10.7554","volume":"2","author":[{"given":"Xing","family":"Zhang","sequence":"first","affiliation":[{"name":"California NanoSystems Institute, University of California, Los Angeles, Los Angeles, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huatao","family":"Guo","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, United 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