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| | ==Coevolution of the ATPase ClpV, the TssB-TssC Sheath and the Accessory HsiE Protein Distinguishes Two Type VI Secretion Classes== | | ==Coevolution of the ATPase ClpV, the TssB-TssC Sheath and the Accessory HsiE Protein Distinguishes Two Type VI Secretion Classes== |
| - | <StructureSection load='4uqy' size='340' side='right' caption='[[4uqy]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='4uqy' size='340' side='right'caption='[[4uqy]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4uqy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4uqy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UQY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uqn|4uqn]], [[4uqw|4uqw]], [[4uqx|4uqx]], [[4uqz|4uqz]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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=4uqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqy RCSB], [http://www.ebi.ac.uk/pdbsum/4uqy PDBsum]</span></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=4uqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqy OCA], [https://pdbe.org/4uqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uqy RCSB], [https://www.ebi.ac.uk/pdbsum/4uqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TSSB1_PSEAE TSSB1_PSEAE] Core component of the H1 type VI (H1-T6SS) secretion system that plays a role in the release of toxins targeting both eukaryotic and prokaryotic species. Forms the sheath of the structure by assembling into tubules together with TssC1 resulting in the stacking of cogwheel-like structures showing predominantly a 12-fold symmetry (PubMed:23341461, PubMed:25305017, PubMed:22906320). The sheath contracts to provide the energy needed for effector delivery (PubMed:29307484).<ref>PMID:22906320</ref> <ref>PMID:23341461</ref> <ref>PMID:25305017</ref> <ref>PMID:29307484</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 4uqy" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Filloux, A.]] | + | [[Category: Large Structures]] |
| - | [[Category: Forster, A.]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Freemont, P S.]] | + | [[Category: Filloux A]] |
| - | [[Category: Lossi, N S.]] | + | [[Category: Forster A]] |
| - | [[Category: Manoli, E.]] | + | [[Category: Freemont PS]] |
| - | [[Category: Planamente, S.]] | + | [[Category: Lossi NS]] |
| - | [[Category: Bacterial]] | + | [[Category: Manoli E]] |
| - | [[Category: Disassembly]] | + | [[Category: Planamente S]] |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Regulation]]
| + | |
| - | [[Category: Secretion]]
| + | |
| - | [[Category: Sheath]]
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| Structural highlights
Function
TSSB1_PSEAE Core component of the H1 type VI (H1-T6SS) secretion system that plays a role in the release of toxins targeting both eukaryotic and prokaryotic species. Forms the sheath of the structure by assembling into tubules together with TssC1 resulting in the stacking of cogwheel-like structures showing predominantly a 12-fold symmetry (PubMed:23341461, PubMed:25305017, PubMed:22906320). The sheath contracts to provide the energy needed for effector delivery (PubMed:29307484).[1] [2] [3] [4]
Publication Abstract from PubMed
The type VI secretion system (T6SS) is a bacterial nanomachine for the transport of effector molecules into prokaryotic and eukaryotic cells. It involves the assembly of a tubular structure composed of TssB and TssC that is similar to the tail sheath of bacteriophages. The sheath contracts to provide the energy needed for effector delivery. The AAA+ ATPase ClpV disassembles the contracted sheath, which resets the systems for reassembly of an extended sheath that is ready to fire again. This mechanism is crucial for T6SS function. In Vibrio cholerae, ClpV binds the N terminus of TssC within a hydrophobic groove. In this study, we resolved the crystal structure of the N-terminal domain of Pseudomonas aeruginosa ClpV1 and observed structural alterations in the hydrophobic groove. The modification in the ClpV1 groove is matched by a change in the N terminus of TssC, suggesting the existence of distinct T6SS classes. An accessory T6SS component, TagJ/HsiE, exists predominantly in one of the classes. Using bacterial two-hybrid approaches, we showed that the P. aeruginosa homolog HsiE1 interacts strongly with ClpV1. We then resolved the crystal structure of HsiE1 in complex with the N terminus of HsiB1, a TssB homolog and component of the contractile sheath. Phylogenetic analysis confirmed that these differences distinguish T6SS classes that resulted from a functional co-evolution between TssB, TssC, TagJ/HsiE and ClpV. The interaction of TagJ/HsiE with the sheath as well as with ClpV suggests an alternative mode of disassembly in which HsiE recruits the ATPase to the sheath.
Coevolution of the ATPase ClpV, the Sheath Proteins TssB and TssC and the Accessory Protein TagJ/HsiE1 Distinguishes Type VI Secretion Classes.,Forster A, Planamente S, Manoli E, Lossi NS, Freemont PS, Filloux A J Biol Chem. 2014 Oct 10. pii: jbc.M114.600510. PMID:25305017[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lossi NS, Manoli E, Simpson P, Jones C, Hui K, Dajani R, Coulthurst SJ, Freemont P, Filloux A. The archetype Pseudomonas aeruginosa proteins TssB and TagJ form a novel subcomplex in the bacterial type VI secretion system. Mol Microbiol. 2012 Oct;86(2):437-56. PMID:22906320 doi:10.1111/j.1365-2958.2012.08204.x
- ↑ Lossi NS, Manoli E, Förster A, Dajani R, Pape T, Freemont P, Filloux A. The HsiB1C1 (TssB-TssC) complex of the Pseudomonas aeruginosa type VI secretion system forms a bacteriophage tail sheathlike structure. J Biol Chem. 2013 Mar 15;288(11):7536-7548. PMID:23341461 doi:10.1074/jbc.M112.439273
- ↑ Forster A, Planamente S, Manoli E, Lossi NS, Freemont PS, Filloux A. Coevolution of the ATPase ClpV, the Sheath Proteins TssB and TssC and the Accessory Protein TagJ/HsiE1 Distinguishes Type VI Secretion Classes. J Biol Chem. 2014 Oct 10. pii: jbc.M114.600510. PMID:25305017 doi:http://dx.doi.org/10.1074/jbc.M114.600510
- ↑ Salih O, He S, Planamente S, Stach L, MacDonald JT, Manoli E, Scheres SHW, Filloux A, Freemont PS. Atomic Structure of Type VI Contractile Sheath from Pseudomonas aeruginosa. Structure. 2017 Dec 21. pii: S0969-2126(17)30404-5. doi:, 10.1016/j.str.2017.12.005. PMID:29307484 doi:http://dx.doi.org/10.1016/j.str.2017.12.005
- ↑ Forster A, Planamente S, Manoli E, Lossi NS, Freemont PS, Filloux A. Coevolution of the ATPase ClpV, the Sheath Proteins TssB and TssC and the Accessory Protein TagJ/HsiE1 Distinguishes Type VI Secretion Classes. J Biol Chem. 2014 Oct 10. pii: jbc.M114.600510. PMID:25305017 doi:http://dx.doi.org/10.1074/jbc.M114.600510
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