View source for 3qq2


==Crystal Structure of the Beta Domain of the Bordetella Autotransporter Brka==
<StructureSection load='3qq2' size='340' side='right'caption='[[3qq2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qq2]] is a 3 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=3QQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QQ2 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]] 3&#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=3qq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qq2 OCA], [https://pdbe.org/3qq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qq2 RCSB], [https://www.ebi.ac.uk/pdbsum/3qq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qq2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BRKA_BORPE BRKA_BORPE] Inhibits the classical pathway of complement activation and prevents accumulation of deposited C4.<ref>PMID:11292725</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Whooping cough (pertussis) is a highly contagious acute respiratory illness of humans caused by the Gram-negative bacterial pathogen Bordetella pertussis. The AT (autotransporter) BrkA (Bordetella serum-resistance killing protein A) is an important B. pertussis virulence factor that confers serum resistance and mediates adherence. In the present study, we have solved the crystal structure of the BrkA beta-domain at 3 A (1 A=0.1 nm) resolution. Special features are a hairpin-like structure formed by the external loop L4, which is observed fortuitously sitting inside the pore of the crystallographic adjacent beta-domain, and a previously undiscovered hydrophobic cavity formed by patches on loop L4 and beta-strands S5 and S6. This adopts a ubiquitous structure characteristic of all AT beta-domains. Mutagenesis studies have demonstrated that the hairpin-like structure and hydrophobic cavity are crucial for BrkA passenger domain (virulence effector) translocation. This structure helps in understanding the molecular mechanism of AT assembly and secretion and provides a potential target for anti-pertussis drug design.

Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the beta-domain pore.,Zhai Y, Zhang K, Huo Y, Zhu Y, Zhou Q, Lu J, Black I, Pang X, Roszak AW, Zhang X, Isaacs NW, Sun F Biochem J. 2011 May 1;435(3):577-87. PMID:21306302<ref>PMID:21306302</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qq2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bordetella pertussis]]
[[Category: Large Structures]]
[[Category: Huo Y]]
[[Category: Sun F]]
[[Category: Zhai Y]]
[[Category: Zhang K]]