5x1h

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==Structure of Legionella pneumophila DotN==
==Structure of Legionella pneumophila DotN==
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<StructureSection load='5x1h' size='340' side='right' caption='[[5x1h]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='5x1h' size='340' side='right'caption='[[5x1h]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5x1h]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X1H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5x1h]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X1H FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.005&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x1e|5x1e]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x1h OCA], [http://pdbe.org/5x1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x1h RCSB], [http://www.ebi.ac.uk/pdbsum/5x1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x1h ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5x1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x1h OCA], [https://pdbe.org/5x1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x1h RCSB], [https://www.ebi.ac.uk/pdbsum/5x1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x1h ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/DOTN_LEGPH DOTN_LEGPH] Component of the Dot/Icm type IVB secretion system (T4BSS), which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:17040490, PubMed:22694730, PubMed:32513920). Part of a subcomplex which recruits effector proteins and delivers them to the core transmembrane subcomplex (PubMed:32513920).<ref>PMID:17040490</ref> <ref>PMID:22694730</ref> <ref>PMID:32513920</ref>
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Many bacteria, including Legionella pneumophila, rely on the type IV secretion system to translocate a repertoire of effector proteins into the hosts for their survival and growth. Type IV coupling protein (T4CP) is a hexameric ATPase that links translocating substrates to the transenvelope secretion conduit. Yet, how a large number of effector proteins are selectively recruited and processed by T4CPs remains enigmatic. DotL, the T4CP of L. pneumophila, contains an ATPase domain and a C-terminal extension whose function is unknown. Unlike T4CPs involved in plasmid DNA translocation, DotL appeared to function by forming a multiprotein complex with four other proteins. Here, we show that the C-terminal extension of DotL interacts with DotN, IcmS, IcmW and an additionally identified subunit LvgA, and that this pentameric assembly binds Legionella effector proteins. We determined the crystal structure of this assembly and built an architecture of the T4CP holocomplex by combining a homology model of the ATPase domain of DotL. The holocomplex is a hexamer of a bipartite structure composed of a membrane-proximal ATPase domain and a membrane-distal substrate-recognition assembly. The presented information demonstrates the architecture and functional dissection of the multiprotein T4CP complexes and provides important insights into their substrate recruitment and processing.
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Architecture of the type IV coupling protein complex of Legionella pneumophila.,Kwak MJ, Kim JD, Kim H, Kim C, Bowman JW, Kim S, Joo K, Lee J, Jin KS, Kim YG, Lee NK, Jung JU, Oh BH Nat Microbiol. 2017 Jul 17;2:17114. doi: 10.1038/nmicrobiol.2017.114. PMID:28714967<ref>PMID:28714967</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5x1h" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Kwak, M J]]
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[[Category: Large Structures]]
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[[Category: Oh, B H]]
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[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
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[[Category: Coupling protein complex]]
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[[Category: Kwak MJ]]
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[[Category: Effector translocation]]
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[[Category: Oh BH]]
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[[Category: Protein transport]]
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[[Category: Type iv secretion system]]
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Current revision

Structure of Legionella pneumophila DotN

PDB ID 5x1h

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