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| | <StructureSection load='6rae' size='340' side='right'caption='[[6rae]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='6rae' size='340' side='right'caption='[[6rae]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rae]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RAE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RAE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rae]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._SL1344 Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RAE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 2.049Å</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=6rae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rae OCA], [http://pdbe.org/6rae PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rae RCSB], [http://www.ebi.ac.uk/pdbsum/6rae PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rae ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6rae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rae OCA], [https://pdbe.org/6rae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rae RCSB], [https://www.ebi.ac.uk/pdbsum/6rae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rae ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SCTN1_SALTY SCTN1_SALTY] ATPase component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:15060043, PubMed:16208377, PubMed:26170413). Acts as a molecular motor to provide the energy that is required for the export of proteins (Probable). Required for type III secretion apparatus (T3SA) formation, proper protein secretion, host cell invasion and virulence (PubMed:8045880, PubMed:14762212, PubMed:15060043, PubMed:26170413). May play a critical role in T3SS substrate recognition, disassembly of the effector/chaperone complex and unfolding of the effector in an ATP-dependent manner prior to secretion (PubMed:16208377). Releases the effector protein SptP from the chaperone SicP in an ATP-dependent manner (PubMed:16208377).<ref>PMID:14762212</ref> <ref>PMID:15060043</ref> <ref>PMID:16208377</ref> <ref>PMID:26170413</ref> <ref>PMID:8045880</ref> <ref>PMID:8045880</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bernal, I]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]] |
| - | [[Category: Flacht, L]] | + | [[Category: Bernal I]] |
| - | [[Category: Kolbe, M]] | + | [[Category: Flacht L]] |
| - | [[Category: Lunelli, M]] | + | [[Category: Kolbe M]] |
| - | [[Category: Roemermann, J]] | + | [[Category: Lunelli M]] |
| - | [[Category: Uetrecht, C]] | + | [[Category: Roemermann J]] |
| - | [[Category: Atpase]]
| + | [[Category: Uetrecht C]] |
| - | [[Category: Bacterial pathogenesis]]
| + | |
| - | [[Category: Crystallography]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Salmonella enterica]]
| + | |
| Structural highlights
Function
SCTN1_SALTY ATPase component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:15060043, PubMed:16208377, PubMed:26170413). Acts as a molecular motor to provide the energy that is required for the export of proteins (Probable). Required for type III secretion apparatus (T3SA) formation, proper protein secretion, host cell invasion and virulence (PubMed:8045880, PubMed:14762212, PubMed:15060043, PubMed:26170413). May play a critical role in T3SS substrate recognition, disassembly of the effector/chaperone complex and unfolding of the effector in an ATP-dependent manner prior to secretion (PubMed:16208377). Releases the effector protein SptP from the chaperone SicP in an ATP-dependent manner (PubMed:16208377).[1] [2] [3] [4] [5] [6]
Publication Abstract from PubMed
Translocation of virulence effector proteins through the type III secretion system (T3SS) is essential for the virulence of many medically relevant Gram-negative bacteria. The T3SS ATPases are conserved components that specifically recognize chaperone-effector complexes and energize effector secretion through the system. It is thought that functional T3SS ATPases assemble into a cylindrical structure maintained by their N-terminal domains. Using SEC-MALS and native mass spectrometry, we show that in the absence of the N-terminal oligomerization domain the Salmonella T3SS ATPase InvC can form monomers and dimers in solution. We also present for the first time a 2.05 a resolution crystal structure of InvC lacking the oligomerization domain (InvCDelta79) and map the amino acids suggested for ATPase intersubunit interaction, binding to other T3SS proteins and chaperone-effector recognition. Furthermore, we validate the InvC ATP binding site by co-crystallization of InvCDelta79 with ATPgammaS (2.65 a) and ADP (2.80 a). Upon ATP-analogue recognition, these structures reveal remodeling of the ATP-binding site and conformational changes of two loops located outside of the catalytic site. Both loops face the central pore of the predicted InvC cylinder and are essential for the function of the T3SS ATPase. Our results present a fine functional and structural correlation of InvC and provide further details of the homo-oligomerization process and ATP-dependent conformational changes underlying the T3SS ATPase activity. This article is protected by copyright. All rights reserved.
Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC.,Bernal I, Romermann J, Flacht L, Lunelli M, Uetrecht C, Kolbe M Protein Sci. 2019 Aug 8. doi: 10.1002/pro.3704. PMID:31393998[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McKinney JS, Zhang H, Kubori T, Galán JE, Altman S. Disruption of type III secretion in Salmonella enterica serovar Typhimurium by external guide sequences. Nucleic Acids Res. 2004 Feb 3;32(2):848-54. PMID:14762212 doi:10.1093/nar/gkh219
- ↑ Akeda Y, Galán JE. Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains. J Bacteriol. 2004 Apr;186(8):2402-12. PMID:15060043 doi:10.1128/JB.186.8.2402-2412.2004
- ↑ Akeda Y, Galán JE. Chaperone release and unfolding of substrates in type III secretion. Nature. 2005 Oct 6;437(7060):911-5. PMID:16208377 doi:10.1038/nature03992
- ↑ Kato J, Lefebre M, Galán JE. Structural Features Reminiscent of ATP-Driven Protein Translocases Are Essential for the Function of a Type III Secretion-Associated ATPase. J Bacteriol. 2015 Sep;197(18):3007-14. PMID:26170413 doi:10.1128/JB.00434-15
- ↑ Eichelberg K, Ginocchio CC, Galán JE. Molecular and functional characterization of the Salmonella typhimurium invasion genes invB and invC: homology of InvC to the F0F1 ATPase family of proteins. J Bacteriol. 1994 Aug;176(15):4501-10. PMID:8045880 doi:10.1128/jb.176.15.4501-4510.1994
- ↑ Eichelberg K, Ginocchio CC, Galán JE. Molecular and functional characterization of the Salmonella typhimurium invasion genes invB and invC: homology of InvC to the F0F1 ATPase family of proteins. J Bacteriol. 1994 Aug;176(15):4501-10. PMID:8045880 doi:10.1128/jb.176.15.4501-4510.1994
- ↑ Bernal I, Romermann J, Flacht L, Lunelli M, Uetrecht C, Kolbe M. Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC. Protein Sci. 2019 Aug 8. doi: 10.1002/pro.3704. PMID:31393998 doi:http://dx.doi.org/10.1002/pro.3704
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