4jiv

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==VCA0105 PAAR-repeat protein from Vibrio cholerae in complex with a VgrG-like beta-helix that is based on a fragment of T4 gp5==
==VCA0105 PAAR-repeat protein from Vibrio cholerae in complex with a VgrG-like beta-helix that is based on a fragment of T4 gp5==
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<StructureSection load='4jiv' size='340' side='right' caption='[[4jiv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='4jiv' size='340' side='right'caption='[[4jiv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4jiv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4] and [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JIV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JIV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4jiv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JIV 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=ELA:9-OCTADECENOIC+ACID'>ELA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=STE:STEARIC+ACID'>STE</scene>, <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]] 1.903&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k28|1k28]], [[4jiw|4jiw]]</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=ELA:9-OCTADECENOIC+ACID'>ELA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=STE:STEARIC+ACID'>STE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4]), VC_A0105 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</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=4jiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jiv OCA], [https://pdbe.org/4jiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jiv RCSB], [https://www.ebi.ac.uk/pdbsum/4jiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jiv ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></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=4jiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jiv OCA], [http://pdbe.org/4jiv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jiv RCSB], [http://www.ebi.ac.uk/pdbsum/4jiv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jiv ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VG05_BPT4 VG05_BPT4]] Tail-associated lysozyme essential for localized hydrolysis of bacterial cell wall necessary for viral DNA injection. The needle-like gp5 protein punctures the outer cell membrane and then digests the peptidoglycan cell wall in the periplasmic space.
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[https://www.uniprot.org/uniprot/NEEDL_BPT4 NEEDL_BPT4] Tail-associated lysozyme of the baseplate hub that is essential for localized hydrolysis of bacterial cell wall necessary for viral DNA injection. The needle-like gp5 protein punctures the outer cell membrane and then digests the peptidoglycan cell wall in the periplasmic space. Involved in the tail assembly.<ref>PMID:12837775</ref> <ref>PMID:21129200</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The bacterial type VI secretion system (T6SS) is a large multicomponent, dynamic macromolecular machine that has an important role in the ecology of many Gram-negative bacteria. T6SS is responsible for translocation of a wide range of toxic effector molecules, allowing predatory cells to kill both prokaryotic as well as eukaryotic prey cells. The T6SS organelle is functionally analogous to contractile tails of bacteriophages and is thought to attack cells by initially penetrating them with a trimeric protein complex called the VgrG spike. Neither the exact protein composition of the T6SS organelle nor the mechanisms of effector selection and delivery are known. Here we report that proteins from the PAAR (proline-alanine-alanine-arginine) repeat superfamily form a sharp conical extension on the VgrG spike, which is further involved in attaching effector domains to the spike. The crystal structures of two PAAR-repeat proteins bound to VgrG-like partners show that these proteins sharpen the tip of the T6SS spike complex. We demonstrate that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae and Acinetobacter baylyi. Our results indicate a new model of the T6SS organelle in which the VgrG-PAAR spike complex is decorated with multiple effectors that are delivered simultaneously into target cells in a single contraction-driven translocation event.
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PAAR-repeat proteins sharpen and diversify the type VI secretion system spike.,Shneider MM, Buth SA, Ho BT, Basler M, Mekalanos JJ, Leiman PG Nature. 2013 Aug 15;500(7462):350-3. doi: 10.1038/nature12453. Epub 2013 Aug 7. PMID:23925114<ref>PMID:23925114</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 4jiv" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bpt4]]
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[[Category: Escherichia virus T4]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
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[[Category: Vibch]]
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[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
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[[Category: Buth, S A]]
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[[Category: Buth SA]]
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[[Category: Leiman, P G]]
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[[Category: Leiman PG]]
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[[Category: Shneider, M M]]
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[[Category: Shneider MM]]
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[[Category: Beta-helix]]
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[[Category: Cell puncturing device]]
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[[Category: Hydrolase-protein binding complex]]
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[[Category: Membrane piercing]]
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[[Category: Paar-repeat motif]]
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[[Category: T4 gp5]]
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[[Category: T6ss spike]]
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[[Category: Type vi secretion system]]
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[[Category: Vgrg tip]]
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[[Category: Vibrio cholerae vgrg2]]
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Current revision

VCA0105 PAAR-repeat protein from Vibrio cholerae in complex with a VgrG-like beta-helix that is based on a fragment of T4 gp5

PDB ID 4jiv

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