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6n38

From Proteopedia

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Current revision (09:20, 20 March 2024) (edit) (undo)
 
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<SX load='6n38' size='340' side='right' viewer='molstar' caption='[[6n38]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<SX load='6n38' size='340' side='right' viewer='molstar' caption='[[6n38]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6n38]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Eaec_042 Eaec 042]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N38 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6N38 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6n38]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_042 Escherichia coli 042]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N38 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EC042_4542 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216592 EAEC 042]), EC042_4543 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216592 EAEC 042]), EC042_4526 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216592 EAEC 042])</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=6n38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n38 OCA], [https://pdbe.org/6n38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n38 RCSB], [https://www.ebi.ac.uk/pdbsum/6n38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n38 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6n38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n38 OCA], [http://pdbe.org/6n38 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n38 RCSB], [http://www.ebi.ac.uk/pdbsum/6n38 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n38 ProSAT]</span></td></tr>
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</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/D3GUX3_ECO44 D3GUX3_ECO44]
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Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the baseplate remain unknown. Here, we report the 3.7 A resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS baseplate architecture.
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Structure of the type VI secretion system TssK-TssF-TssG baseplate subcomplex revealed by cryo-electron microscopy.,Park YJ, Lacourse KD, Cambillau C, DiMaio F, Mougous JD, Veesler D Nat Commun. 2018 Dec 19;9(1):5385. doi: 10.1038/s41467-018-07796-5. PMID:30568167<ref>PMID:30568167</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 6n38" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Eaec 042]]
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[[Category: Escherichia coli 042]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cambillau, C]]
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[[Category: Cambillau C]]
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[[Category: DiMaio, F]]
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[[Category: DiMaio F]]
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[[Category: Lacourse, K D]]
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[[Category: Lacourse KD]]
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[[Category: Mougous, J D]]
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[[Category: Mougous JD]]
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[[Category: Park, Y J]]
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[[Category: Park YJ]]
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[[Category: Structural genomic]]
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[[Category: Veesler D]]
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[[Category: Veesler, D]]
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[[Category: Baseplate]]
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[[Category: Enteroaggregative e. coli]]
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[[Category: Protein secretion]]
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[[Category: Protein transport]]
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[[Category: Ssgcid]]
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[[Category: Type vi secretion system]]
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Current revision

Structure of the type VI secretion system TssK-TssF-TssG baseplate subcomplex revealed by cryo-electron microscopy - full map sharpened

6n38, resolution 3.70Å

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