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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4jtm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_ETEC_H10407 Escherichia coli ETEC H10407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JTM FirstGlance]. <br>
<table><tr><td colspan='2'>[[4jtm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_ETEC_H10407 Escherichia coli ETEC H10407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JTM 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=4jtm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jtm OCA], [https://pdbe.org/4jtm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jtm RCSB], [https://www.ebi.ac.uk/pdbsum/4jtm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jtm 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]] 1.43&#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=4jtm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jtm OCA], [https://pdbe.org/4jtm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jtm RCSB], [https://www.ebi.ac.uk/pdbsum/4jtm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jtm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/GSPD2_ECOH1 GSPD2_ECOH1] Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable).<ref>PMID:22585966</ref> <ref>PMID:23820381</ref> <ref>PMID:29632366</ref>  
[https://www.uniprot.org/uniprot/GSPD2_ECOH1 GSPD2_ECOH1] Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable).<ref>PMID:22585966</ref> <ref>PMID:23820381</ref> <ref>PMID:29632366</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In many bacteria, secretins from the type II secretion system (T2SS) function as outer membrane gated channels that enable passage of folded proteins from the periplasm into the extracellular milieu. Cryo-electron microscopy of the T2SS secretin GspD revealed previously the dodecameric cylindrical architecture of secretins, and crystal structures of periplasmic secretin domains showed a modular domain organization. However, no high-resolution experimental data has as yet been provided about how the entire T2SS secretin or its domains are organized in a cylindrical fashion. Here we present a crystal structure of the N0 domain of the T2SS secretin GspD from enterotoxigenic Escherichia coli containing a helix with 12 subunits per turn. The helix has an outer diameter of approximately 125A and a pitch of only 24A which suggests a model of a cylindrical dodecameric N0 ring whose dimensions correspond with the cryo-electron microscopy map of Vibrio cholerae GspD. The N0 domain is known to interact with the HR domain of the inner membrane T2SS protein GspC. When the new N0 ring model is combined with the known N0.HR crystal structure, a dodecameric double-ring of twelve N0-HR heterodimers is obtained. In contrast, the previously observed compact N0-N1 GspD module is not compatible with the N0 ring. Interestingly, a N0-N1 T3SS homolog is compatible with forming a N0-N1 dodecameric ring, due to a different N0-vs-N1 orientation. This suggests that the dodecameric N0 ring is an important feature of T2SS secretins with periplasmic domains undergoing considerable motions during exoprotein translocation.
A dodecameric ring-like structure of the N0 domain of the type II secretin from enterotoxigenic Escherichia coli.,Korotkov KV, Delarosa JR, Hol WG J Struct Biol. 2013 Jun 29. pii: S1047-8477(13)00168-8. doi:, 10.1016/j.jsb.2013.06.013. PMID:23820381<ref>PMID:23820381</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4jtm" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 12:06, 1 March 2024

Structure of the N0 domain of the type II secretin from enterotoxigenic Escherichia coli

4jtm, resolution 1.43Å

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