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| <StructureSection load='4y7l' size='340' side='right'caption='[[4y7l]], [[Resolution|resolution]] 1.51Å' scene=''> | | <StructureSection load='4y7l' size='340' side='right'caption='[[4y7l]], [[Resolution|resolution]] 1.51Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4y7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_2-156-04_s3_c3 Escherichia coli 2-156-04_s3_c3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y7L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y7l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_2-156-04_S3_C3 Escherichia coli 2-156-04_S3_C3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y7L FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AC43_2230 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1444178 Escherichia coli 2-156-04_S3_C3])</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=4y7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7l OCA], [https://pdbe.org/4y7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y7l RCSB], [https://www.ebi.ac.uk/pdbsum/4y7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7l ProSAT]</span></td></tr> |
- | <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=4y7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7l OCA], [http://pdbe.org/4y7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y7l RCSB], [http://www.ebi.ac.uk/pdbsum/4y7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7l ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/A0A0M3KL15_ECOLX A0A0M3KL15_ECOLX] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Escherichia coli 2-156-04_s3_c3]] | + | [[Category: Escherichia coli 2-156-04_S3_C3]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Cambillau, C]] | + | [[Category: Cambillau C]] |
- | [[Category: Durand, E]] | + | [[Category: Durand E]] |
- | [[Category: Nguyen, V S]] | + | [[Category: Nguyen VS]] |
- | [[Category: Roussel, A]] | + | [[Category: Roussel A]] |
- | [[Category: Spinelli, S]] | + | [[Category: Spinelli S]] |
- | [[Category: Alpha-beta fold]]
| + | |
- | [[Category: Membrane protein]]
| + | |
- | [[Category: Periplasmic protein]]
| + | |
- | [[Category: Type 6 secretion system]]
| + | |
| Structural highlights
Function
A0A0M3KL15_ECOLX
Publication Abstract from PubMed
Bacteria share their ecological niches with other microbes. The bacterial type VI secretion system is one of the key players in microbial competition, as well as being an important virulence determinant during bacterial infections. It assembles a nano-crossbow-like structure in the cytoplasm of the attacker cell that propels an arrow made of a haemolysin co-regulated protein (Hcp) tube and a valine-glycine repeat protein G (VgrG) spike and punctures the prey's cell wall. The nano-crossbow is stably anchored to the cell envelope of the attacker by a membrane core complex. Here we show that this complex is assembled by the sequential addition of three type VI subunits (Tss)-TssJ, TssM and TssL-and present a structure of the fully assembled complex at 11.6 A resolution, determined by negative-stain electron microscopy. With overall C5 symmetry, this 1.7-megadalton complex comprises a large base in the cytoplasm. It extends in the periplasm via ten arches to form a double-ring structure containing the carboxy-terminal domain of TssM (TssMct) and TssJ that is anchored in the outer membrane. The crystal structure of the TssMct-TssJ complex coupled to whole-cell accessibility studies suggest that large conformational changes induce transient pore formation in the outer membrane, allowing passage of the attacking Hcp tube/VgrG spike.
Biogenesis and structure of a type VI secretion membrane core complex.,Durand E, Nguyen VS, Zoued A, Logger L, Pehau-Arnaudet G, Aschtgen MS, Spinelli S, Desmyter A, Bardiaux B, Dujeancourt A, Roussel A, Cambillau C, Cascales E, Fronzes R Nature. 2015 Jul 30;523(7562):555-60. doi: 10.1038/nature14667. Epub 2015 Jul 22. PMID:26200339[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Durand E, Nguyen VS, Zoued A, Logger L, Pehau-Arnaudet G, Aschtgen MS, Spinelli S, Desmyter A, Bardiaux B, Dujeancourt A, Roussel A, Cambillau C, Cascales E, Fronzes R. Biogenesis and structure of a type VI secretion membrane core complex. Nature. 2015 Jul 30;523(7562):555-60. doi: 10.1038/nature14667. Epub 2015 Jul 22. PMID:26200339 doi:http://dx.doi.org/10.1038/nature14667
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