1rwr: Difference between revisions

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<StructureSection load='1rwr' size='340' side='right'caption='[[1rwr]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
<StructureSection load='1rwr' size='340' side='right'caption='[[1rwr]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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='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>
</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>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FHAB_BORPE FHAB_BORPE]] Evidence for a role in host-cell binding and infection.  
[https://www.uniprot.org/uniprot/FHAB_BORPE FHAB_BORPE] Evidence for a role in host-cell binding and infection.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 1rwr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterium tussis-convulsivae lehmann and neumann 1927]]
[[Category: Bordetella pertussis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Clantin, B]]
[[Category: Clantin B]]
[[Category: Villeret, V]]
[[Category: Villeret V]]
[[Category: Adhesin]]
[[Category: Beta-helix]]
[[Category: Cell adhesion]]
[[Category: Filamentous hemagglutinin]]
[[Category: Tps domain]]
[[Category: Type v secretion]]

Latest revision as of 13:29, 13 March 2024

Crystal structure of filamentous hemagglutinin secretion domain

1rwr, resolution 1.72Å

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