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| | <StructureSection load='3eb8' size='340' side='right'caption='[[3eb8]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3eb8' size='340' side='right'caption='[[3eb8]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3eb8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EB8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3eb8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EB8 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">virA, CP0181, pWR501_0191 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</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]] 2.4Å</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=3eb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eb8 OCA], [https://pdbe.org/3eb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eb8 RCSB], [https://www.ebi.ac.uk/pdbsum/3eb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eb8 ProSAT]</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=3eb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eb8 OCA], [https://pdbe.org/3eb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eb8 RCSB], [https://www.ebi.ac.uk/pdbsum/3eb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eb8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/VIRA_SHIFL VIRA_SHIFL]] Alpha-tubulin-specific protease that is required for entry into epithelial cells and for subsequent intra- and intercellular spreading. Contributes to bacterial entry into epithelial cells by inducing microtubule (MT) destabilization and the formation of membrane ruffles. The membrane ruffling evoked by VirA results from the activation of host rac1, which is associated with the destruction of MT networks. Creates a tunnel inside the host cell cytoplasm by breaking down the microtubule infrastructure. This facilitates the bacterium's movement through the cytoplasm and also helps other bacteria move faster during the invasion of the eukaryotic cell. Is absolutely required for virulence.<ref>PMID:7494473</ref> <ref>PMID:12065406</ref> <ref>PMID:17095701</ref>
| + | [https://www.uniprot.org/uniprot/VIRA_SHIFL VIRA_SHIFL] Alpha-tubulin-specific protease that is required for entry into epithelial cells and for subsequent intra- and intercellular spreading. Contributes to bacterial entry into epithelial cells by inducing microtubule (MT) destabilization and the formation of membrane ruffles. The membrane ruffling evoked by VirA results from the activation of host rac1, which is associated with the destruction of MT networks. Creates a tunnel inside the host cell cytoplasm by breaking down the microtubule infrastructure. This facilitates the bacterium's movement through the cytoplasm and also helps other bacteria move faster during the invasion of the eukaryotic cell. Is absolutely required for virulence.<ref>PMID:7494473</ref> <ref>PMID:12065406</ref> <ref>PMID:17095701</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Shigella paradysenteriae weldin 1927]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Germane, K L]] | + | [[Category: Shigella flexneri]] |
| - | [[Category: Spiller, B W]] | + | [[Category: Germane KL]] |
| - | [[Category: Alpha helix]] | + | [[Category: Spiller BW]] |
| - | [[Category: Beta sheet]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Thiol protease]]
| + | |
| - | [[Category: Virulence]]
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| Structural highlights
Function
VIRA_SHIFL Alpha-tubulin-specific protease that is required for entry into epithelial cells and for subsequent intra- and intercellular spreading. Contributes to bacterial entry into epithelial cells by inducing microtubule (MT) destabilization and the formation of membrane ruffles. The membrane ruffling evoked by VirA results from the activation of host rac1, which is associated with the destruction of MT networks. Creates a tunnel inside the host cell cytoplasm by breaking down the microtubule infrastructure. This facilitates the bacterium's movement through the cytoplasm and also helps other bacteria move faster during the invasion of the eukaryotic cell. Is absolutely required for virulence.[1] [2] [3]
Publication Abstract from PubMed
VirA, an essential virulence factor in Shigella disease pathogenesis, is involved in the uptake, motility, and cell-to-cell spread of Shigella organisms within the human host. These functions have been attributed to a VirA protease activity and a mechanism of microtubule destruction via tubulin degradation [Yoshida, S., et al. (2006) Science 314, 985-989]. We report functional and crystallographic data indicating a novel VirA structure that lacks these activities but highlights the homology to the EspG virulence factor of pathogenic Escherichia coli.
Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules.,Germane KL, Ohi R, Goldberg MB, Spiller BW Biochemistry. 2008 Sep 30;47(39):10241-3. Epub 2008 Sep 3. PMID:18763811[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Uchiya K, Tobe T, Komatsu K, Suzuki T, Watarai M, Fukuda I, Yoshikawa M, Sasakawa C. Identification of a novel virulence gene, virA, on the large plasmid of Shigella, involved in invasion and intercellular spreading. Mol Microbiol. 1995 Jul;17(2):241-50. PMID:7494473
- ↑ Yoshida S, Katayama E, Kuwae A, Mimuro H, Suzuki T, Sasakawa C. Shigella deliver an effector protein to trigger host microtubule destabilization, which promotes Rac1 activity and efficient bacterial internalization. EMBO J. 2002 Jun 17;21(12):2923-35. PMID:12065406 doi:10.1093/emboj/cdf319
- ↑ Yoshida S, Handa Y, Suzuki T, Ogawa M, Suzuki M, Tamai A, Abe A, Katayama E, Sasakawa C. Microtubule-severing activity of Shigella is pivotal for intercellular spreading. Science. 2006 Nov 10;314(5801):985-9. PMID:17095701 doi:10.1126/science.1133174
- ↑ Germane KL, Ohi R, Goldberg MB, Spiller BW. Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules. Biochemistry. 2008 Sep 30;47(39):10241-3. Epub 2008 Sep 3. PMID:18763811 doi:10.1021/bi801533k
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