4nrh
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nrh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_pneumoniae Chlamydia pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NRH FirstGlance]. <br> | <table><tr><td colspan='2'>[[4nrh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_pneumoniae Chlamydia pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NRH FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=4nrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrh OCA], [https://pdbe.org/4nrh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nrh RCSB], [https://www.ebi.ac.uk/pdbsum/4nrh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrh 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=4nrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrh OCA], [https://pdbe.org/4nrh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nrh RCSB], [https://www.ebi.ac.uk/pdbsum/4nrh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q9Z8L4_CHLPN Q9Z8L4_CHLPN] | [https://www.uniprot.org/uniprot/Q9Z8L4_CHLPN Q9Z8L4_CHLPN] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Many Gram-negative bacteria use Type Three Secretion Systems (T3SS) to deliver effector proteins into host cells. These protein delivery machines are composed of cytosolic components that recognize substrates and generate the force needed for translocation, the secretion conduit, formed by a needle complex and associated membrane spanning basal body, and translocators that form the pore in the target cell. A defined order of secretion in which needle component proteins are secreted first, followed by translocators, and finally effectors, is necessary for this system to be effective. While the secreted effectors vary significantly between organisms, the approximately 20 individual protein components that form the T3SS are conserved in many pathogenic bacteria. One such conserved protein, referred to as either a plug or gatekeeper, is necessary to prevent unregulated effector release and to allow efficient translocator secretion. The mechanism by which translocator secretion is promoted while effector release is inhibited by gatekeepers is unknown. We present the structure of the Chlamydial gatekeeper, CopN, bound to a translocator-specific chaperone. The structure identifies a previously unknown interface between gatekeepers and translocator chaperones and reveals that in the gatekeeper-chaperone complex the canonical translocator-binding groove is free to bind translocators. Structure-based mutagenesis of the homologous complex in Shigella reveals that the gatekeeper-chaperone-translocator complex is essential for translocator secretion and for the ordered secretion of translocators prior to effectors. | ||
| - | |||
| - | A gatekeeper chaperone complex directs translocator secretion during type three secretion.,Archuleta TL, Spiller BW PLoS Pathog. 2014 Nov 6;10(11):e1004498. doi: 10.1371/journal.ppat.1004498., eCollection 2014 Nov. PMID:25375170<ref>PMID:25375170</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4nrh" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
CopN-Scc3 complex
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