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New page: left|200px<br /><applet load="1rwr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rwr, resolution 1.72Å" /> '''Crystal structure of...
 
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[[Image:1rwr.gif|left|200px]]<br /><applet load="1rwr" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rwr, resolution 1.72&Aring;" />
'''Crystal structure of filamentous hemagglutinin secretion domain'''<br />


==Overview==
==Crystal structure of filamentous hemagglutinin secretion domain==
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.
<StructureSection load='1rwr' size='340' side='right'caption='[[1rwr]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rwr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FHAB_BORPE FHAB_BORPE] Evidence for a role in host-cell binding and infection.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rw/1rwr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rwr ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1RWR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RWR OCA].
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15079085 15079085]
[[Category: Bordetella pertussis]]
[[Category: Bordetella pertussis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Clantin, B.]]
[[Category: Clantin B]]
[[Category: Villeret, V.]]
[[Category: Villeret V]]
[[Category: adhesins]]
[[Category: beta-helix]]
[[Category: filamentous hemagglutinin]]
[[Category: tps domain]]
[[Category: type v secretion]]
 
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