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| | ==Crystal structure of the effector-immunity protein complex== | | ==Crystal structure of the effector-immunity protein complex== |
| - | <StructureSection load='4nso' size='340' side='right' caption='[[4nso]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4nso' size='340' side='right'caption='[[4nso]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nso]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NSO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NSO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nso]] is a 2 chain structure with sequence from [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=4NSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NSO FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nsr|4nsr]]</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=4nso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nso OCA], [https://pdbe.org/4nso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nso RCSB], [https://www.ebi.ac.uk/pdbsum/4nso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nso ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VCPCS023_003519, VC_A0123 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH]), VC_A0124 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>
| + | </table> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nso OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nso RCSB], [http://www.ebi.ac.uk/pdbsum/4nso PDBsum]</span></td></tr>
| + | == Function == |
| - | <table> | + | [https://www.uniprot.org/uniprot/VGRG3_VIBCH VGRG3_VIBCH] Part of the type VI secretion system specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (PubMed:23362380, PubMed:23341465). Forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein Hcp. Allows the delivery of the TseL antibacterial toxin to target cells where it exerts its toxicity (PubMed:23362380). Additionally, acts directly as an effector and targets the cell wall peptidoglycan layer of prey cells for degradation via its C-terminus (PubMed:23362380, PubMed:23341465). Toxicity is counteracted by a cognate immunity protein TsiV3 (PubMed:23362380, PubMed:24699653, PubMed:23341465).<ref>PMID:23341465</ref> <ref>PMID:23362380</ref> <ref>PMID:24699653</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4nso" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibch]] | + | [[Category: Large Structures]] |
| - | [[Category: Dong, C.]] | + | [[Category: Vibrio cholerae O1 biovar El Tor str. N16961]] |
| - | [[Category: Helix]] | + | [[Category: Dong C]] |
| - | [[Category: Peptidoglycan]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
VGRG3_VIBCH Part of the type VI secretion system specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (PubMed:23362380, PubMed:23341465). Forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein Hcp. Allows the delivery of the TseL antibacterial toxin to target cells where it exerts its toxicity (PubMed:23362380). Additionally, acts directly as an effector and targets the cell wall peptidoglycan layer of prey cells for degradation via its C-terminus (PubMed:23362380, PubMed:23341465). Toxicity is counteracted by a cognate immunity protein TsiV3 (PubMed:23362380, PubMed:24699653, PubMed:23341465).[1] [2] [3]
Publication Abstract from PubMed
The bacterial type VI secretion system (T6SS) is used by donor cells to inject toxic effectors into receptor cells. The donor cells produce the corresponding immunity proteins to protect themselves against the effector proteins, thereby preventing their self-intoxication. Recently, the C-terminal domain of VgrG3 was identified as a T6SS effector. Information on the molecular mechanism of VgrG3 and its immunity protein TsaB has been lacking. Here, we determined the crystal structures of native TsaB and the VgrG3C-TsaB complex. VgrG3C adopts a canonical phage-T4-lysozyme-like fold. TsaB interacts with VgrG3C through molecular mimicry, and inserts into the VgrG3C pocket. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: VgrG3 and TsaBbind by x-ray crystallography (View interaction) TsaB and TsaBbind by x-ray crystallography (View interaction) VgrG3 and TsaBbind by cosedimentation in solution (View interaction) TsaB and TsaBbind by cosedimentation in solution (1,2) TsaBbinds to VgrG3 by surface plasmon resonance (1, 2, 3, 4, 5, 6, 7) VgrG3 and TsaBbind by molecular sieving (View interaction) TsaB and TsaBbind by molecular sieving (View interaction) VgrG3 and TsaBbind by x ray scattering (View interaction).
Structural basis for recognition of the type VI spike protein VgrG3 by a cognate immunity protein.,Zhang J, Zhang H, Gao Z, Hu H, Dong C, Dong YH FEBS Lett. 2014 May 21;588(10):1891-8. doi: 10.1016/j.febslet.2014.04.016. Epub, 2014 Apr 18. PMID:24751834[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brooks TM, Unterweger D, Bachmann V, Kostiuk B, Pukatzki S. Lytic activity of the Vibrio cholerae type VI secretion toxin VgrG-3 is inhibited by the antitoxin TsaB. J Biol Chem. 2013 Mar 15;288(11):7618-7625. doi: 10.1074/jbc.M112.436725. Epub , 2013 Jan 22. PMID:23341465 doi:http://dx.doi.org/10.1074/jbc.M112.436725
- ↑ Dong TG, Ho BT, Yoder-Himes DR, Mekalanos JJ. Identification of T6SS-dependent effector and immunity proteins by Tn-seq in Vibrio cholerae. Proc Natl Acad Sci U S A. 2013 Feb 12;110(7):2623-8. doi: , 10.1073/pnas.1222783110. Epub 2013 Jan 29. PMID:23362380 doi:http://dx.doi.org/10.1073/pnas.1222783110
- ↑ Yang X, Xu M, Wang Y, Xia P, Wang S, Ye B, Tong L, Jiang T, Fan Z. Molecular mechanism for self-protection against the type VI secretion system in Vibrio cholerae. Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1094-103. doi:, 10.1107/S1399004714001242. Epub 2014 Mar 20. PMID:24699653 doi:http://dx.doi.org/10.1107/S1399004714001242
- ↑ Zhang J, Zhang H, Gao Z, Hu H, Dong C, Dong YH. Structural basis for recognition of the type VI spike protein VgrG3 by a cognate immunity protein. FEBS Lett. 2014 May 21;588(10):1891-8. doi: 10.1016/j.febslet.2014.04.016. Epub, 2014 Apr 18. PMID:24751834 doi:http://dx.doi.org/10.1016/j.febslet.2014.04.016
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