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| | ==Truncated SipD from Salmonella typhimurium== | | ==Truncated SipD from Salmonella typhimurium== |
| - | <StructureSection load='2ym0' size='340' side='right' caption='[[2ym0]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='2ym0' size='340' side='right'caption='[[2ym0]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ym0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YM0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YM0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ym0]] is a 2 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=2YM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YM0 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></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]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ym9|2ym9]], [[3zqe|3zqe]], [[3zqb|3zqb]]</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></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=2ym0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ym0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ym0 RCSB], [http://www.ebi.ac.uk/pdbsum/2ym0 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=2ym0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ym0 OCA], [https://pdbe.org/2ym0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ym0 RCSB], [https://www.ebi.ac.uk/pdbsum/2ym0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ym0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SIPD_SALTY SIPD_SALTY]] Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC.<ref>PMID:8522512</ref> <ref>PMID:9194702</ref> | + | [https://www.uniprot.org/uniprot/SIPD_SALTY SIPD_SALTY] Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC.<ref>PMID:8522512</ref> <ref>PMID:9194702</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 2ym0" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | + | [[Category: Large Structures]] |
| - | [[Category: Kolbe, M]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]] |
| - | [[Category: Lunelli, M]] | + | [[Category: Kolbe M]] |
| - | [[Category: Bacterial pathogenesis]]
| + | [[Category: Lunelli M]] |
| - | [[Category: Cell invasion]]
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| - | [[Category: Host pathogen interaction]]
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| - | [[Category: Needle tip protein]]
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| - | [[Category: T3ss]]
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| - | [[Category: Tip complex]]
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| - | [[Category: Type 3 secretion]]
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| Structural highlights
Function
SIPD_SALTY Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC.[1] [2]
Publication Abstract from PubMed
Many infectious gram-negative bacteria, including Salmonella typhimurium, require a Type Three Secretion System (T3SS) to translocate virulence factors into host cells. The T3SS consists of a membrane protein complex and an extracellular needle together that form a continuous channel. Regulated secretion of virulence factors requires the presence of SipD at the T3SS needle tip in S. typhimurium. Here we report three-dimensional structures of individual SipD, SipD in fusion with the needle subunit PrgI, and of SipD:PrgI in complex with the bile salt, deoxycholate. Assembly of the complex involves major conformational changes in both SipD and PrgI. This rearrangement is mediated via a pi bulge in the central SipD helix and is stabilized by conserved amino acids that may allow for specificity in the assembly and composition of the tip proteins. Five copies each of the needle subunit PrgI and SipD form the T3SS needle tip complex. Using surface plasmon resonance spectroscopy and crystal structure analysis we found that the T3SS needle tip complex binds deoxycholate with micromolar affinity via a cleft formed at the SipD:PrgI interface. In the structure-based three-dimensional model of the T3SS needle tip, the bound deoxycholate faces the host membrane. Recently, binding of SipD with bile salts present in the gut was shown to impede bacterial infection. Binding of bile salts to the SipD:PrgI interface in this particular arrangement may thus inhibit the T3SS function. The structures presented in this study provide insight into the open state of the T3SS needle tip. Our findings present the atomic details of the T3SS arrangement occurring at the pathogen-host interface.
Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands.,Lunelli M, Hurwitz R, Lambers J, Kolbe M PLoS Pathog. 2011 Aug;7(8):e1002163. Epub 2011 Aug 4. PMID:21829362[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kaniga K, Trollinger D, Galan JE. Identification of two targets of the type III protein secretion system encoded by the inv and spa loci of Salmonella typhimurium that have homology to the Shigella IpaD and IpaA proteins. J Bacteriol. 1995 Dec;177(24):7078-85. PMID:8522512
- ↑ Collazo CM, Galan JE. The invasion-associated type III system of Salmonella typhimurium directs the translocation of Sip proteins into the host cell. Mol Microbiol. 1997 May;24(4):747-56. PMID:9194702
- ↑ Lunelli M, Hurwitz R, Lambers J, Kolbe M. Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands. PLoS Pathog. 2011 Aug;7(8):e1002163. Epub 2011 Aug 4. PMID:21829362 doi:10.1371/journal.ppat.1002163
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