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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e9j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E9J FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e9j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E9J FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.03&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4e9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9j OCA], [https://pdbe.org/4e9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e9j RCSB], [https://www.ebi.ac.uk/pdbsum/4e9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9j ProSAT]</span></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=4e9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9j OCA], [https://pdbe.org/4e9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e9j RCSB], [https://www.ebi.ac.uk/pdbsum/4e9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9j ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GSPD_PSEAE GSPD_PSEAE]] Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins.
[https://www.uniprot.org/uniprot/GSPD_PSEAE GSPD_PSEAE] Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The type II secretion system (T2SS) is a multi-protein assembly spanning the inner and outer-membrane in Gram-negative bacteria. It is found in almost all pathogenic bacteria where it contributes to virulence, host tissue colonization and infection. The exoproteins are secreted across the outer-membrane via a large translocation channel, the secretin, which typically adopts a dodecameric structure. These secretin channels have large periplasmic N-terminal domains that reach out into the periplasm for communication with the inner-membrane platform and with a pseudopilus structure that spans the periplasm. Here we report the crystal structure of the N-terminal periplasmic domain of the secretin XcpQ from Pseudomonas aeruginosa, revealing a two-lobe dimeric assembly featuring parallel subunits engaging in well-defined interactions at the tips of each lobe. We have employed structure-based engineering of disulfide bridges and native mass spectrometry to show that the periplasmic domain of XcpQ dimerizes in a concentration dependent manner. Validation of these insights in the context of cellular full-length XcpQ and further evaluation of the functionality of disulfide-linked XcpQ establishes that the basic oligomerization unit of XcpQ is a dimer. This is consistent with the notion that the dodecameric secretin assembles as a hexamer of dimers to ensure correct projection of the N-terminal domains into the periplasm. Therefore, our studies provide a key conceptual advancement in understanding the assembly principles and dynamic function of T2SS secretins, and challenge recent studies reporting monomers as the basic subunit of the secretin oligomer.
 
New insights into the assembly of bacterial secretins: structural studies of the periplasmic domain of XcpQ from Pseudomonas aeruginosa.,Van der Meeren R, Wen Y, Van Gelder P, Tommassen J, Devreese B, Savvides SN J Biol Chem. 2012 Nov 27. PMID:23188826<ref>PMID:23188826</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4e9j" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[General secretion pathway protein 3D structures|General secretion pathway protein 3D structures]]
*[[General secretion pathway protein 3D structures|General secretion pathway protein 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>

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