{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T22:54:47Z","timestamp":1791327287460,"version":"4.3.1"},"reference-count":32,"publisher":"National Academy of Sciences","issue":"16","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2004,4,20]]},"abstract":"<jats:p>\n                    Filamentous hemagglutinin (FHA), the major 230-kDa adhesin of the whooping cough agent\n                    <jats:italic>Bordetella pertussis<\/jats:italic>\n                    , is one of the most efficiently secreted proteins in Gram-negative bacteria. FHA is secreted by means of the two-partner secretion (TPS) pathway. Several important human, animal, and plant pathogens also secrete adhesins and other virulence factors by using this mode of secretion. A TPS system is composed of two separate proteins, with TpsA the secreted protein and TpsB its associated specific outermembrane transporter. All TPS-secreted proteins contain a distinctive N-proximal module essential for secretion, the TPS domain. We report here the 1.7- \u00c5 structure of a functionally secreted 30-kDa N-terminal fragment of FHA. It reveals that the TPS domain folds into a \u03b2-helix, with three extrahelical motifs, a \u03b2-hairpin, a four-stranded \u03b2-sheet, and an N-terminal capping, mostly formed by the nonconserved regions of the TPS domain. The structure thus explains why the TPS domain is able to initiate folding of the \u03b2-helical motifs that form the central domain of the adhesin, because it is itself a \u03b2-helical scaffold. It also contains less conserved extrahelical regions most likely involved in specific properties, such as the recognition of the outer-membrane transporter. This structure is representative of the TPS domains found so far in &gt;100 secreted proteins from pathogenic bacteria. It also provides a mechanistic insight into how protein folding may be linked to secretion in the TPS pathway.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0400291101","type":"journal-article","created":{"date-parts":[[2004,4,12]],"date-time":"2004-04-12T21:04:03Z","timestamp":1081803843000},"page":"6194-6199","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":168,"title":["The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway"],"prefix":"10.1073","volume":"101","author":[{"given":"Bernard","family":"Clantin","sequence":"first","affiliation":[{"name":"Institut F\u00e9d\u00e9ratif de Recherche du Centre National de la Recherche Scientifique 3, Institut National de la Sant\u00e9 et de la Recherche M\u00e9dicale U629, Unit\u00e9 Mixte de Recherche 8525, Centre National de la Recherche Scientifique, Institut de Biologie de Lille, Institut Pasteur de Lille, 1 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