1rwr

<table><tr><td colspan='2'>[[1rwr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_tussis-convulsivae"_lehmann_and_neumann_1927 "bacterium tussis-convulsivae" lehmann and neumann 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RWR FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rwr OCA], [https://pdbe.org/1rwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rwr RCSB], [https://www.ebi.ac.uk/pdbsum/1rwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rwr ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/FHAB_BORPE FHAB_BORPE]] Evidence for a role in host-cell binding and infection.

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== Publication Abstract from PubMed ==

Filamentous hemagglutinin (FHA), the major 230-kDa adhesin of the whooping cough agent Bordetella pertussis, 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- A structure of a functionally secreted 30-kDa N-terminal fragment of FHA. It reveals that the TPS domain folds into a beta-helix, with three extrahelical motifs, a beta-hairpin, a four-stranded beta-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 beta-helical motifs that form the central domain of the adhesin, because it is itself a beta-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.

The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway.,Clantin B, Hodak H, Willery E, Locht C, Jacob-Dubuisson F, Villeret V Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6194-9. Epub 2004 Apr 12. PMID:15079085<ref>PMID:15079085</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1rwr" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacterium tussis-convulsivae lehmann and neumann 1927]]

[[Category: Clantin, B]]

[[Category: Villeret, V]]

[[Category: Type v secretion]]