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Hops share a conserved 25 kDa C\u2010terminal region that is thought to form an autotransporter\u2010like transmembrane domain. Instead, our results show that Hops contain a non\u2010continuous transmembrane domain, composed of seven predicted \u03b2\u2013strands at the C\u2013terminus and one at the N\u2010terminus. Folding and outer membrane localization of the C\u2013terminal \u03b2\u2013domain critically depends on a predicted transmembrane \u03b2\u2010strand within the first 16 N\u2010terminal residues. The N\u2010terminus is shown to reside in the periplasm, and our crystal and small angle X\u2010ray scattering structures for the SabA extracellular domain reveal a conserved coiled\u2010coil stem domain that connects to transmembrane \u03b2\u2010strand 1 and 2. Taken together, our data show that Hop adhesins represent a novel outer membrane protein topology encompassing an OmpA\u2010like 8\u2013stranded \u03b2\u2010barrel that is interrupted by a 15\u2013108 kDa domain inserted inside the first extracellular loop. The insertion of large, folded domains in an extracellular loop is unprecedented in bacterial outer membrane proteins and is expected to have important consequences on how these proteins reach the cell surface.<\/jats:p>","DOI":"10.1111\/mmi.14075","type":"journal-article","created":{"date-parts":[[2018,7,11]],"date-time":"2018-07-11T15:19:34Z","timestamp":1531322374000},"page":"33-46","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":32,"title":["Hop\u2010family <i>Helicobacter<\/i> outer membrane adhesins form a novel class of Type\u00a05\u2010like secretion proteins with an interrupted \u03b2\u2010barrel domain"],"prefix":"10.1111","volume":"110","author":[{"given":"Fanny","family":"Coppens","sequence":"first","affiliation":[{"name":"Structural and Molecular Microbiology VIB\u2010VUB Center for Structural Biology, VIB Brussels Belgium."},{"name":"Structural Biology Brussels Vrije Universiteit Brussel Brussels 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