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| | <StructureSection load='2gdc' size='340' side='right'caption='[[2gdc]], [[Resolution|resolution]] 2.74Å' scene=''> | | <StructureSection load='2gdc' size='340' side='right'caption='[[2gdc]], [[Resolution|resolution]] 2.74Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2gdc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927] and [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GDC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2gdc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GDC FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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]] 2.74Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VCL, VINC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK]), ipaA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</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=2gdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gdc OCA], [https://pdbe.org/2gdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gdc RCSB], [https://www.ebi.ac.uk/pdbsum/2gdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gdc 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=2gdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gdc OCA], [https://pdbe.org/2gdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gdc RCSB], [https://www.ebi.ac.uk/pdbsum/2gdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gdc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/VINC_CHICK VINC_CHICK]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:15229287</ref> <ref>PMID:20584916</ref> <ref>PMID:20086044</ref> [[https://www.uniprot.org/uniprot/IPAA_SHIFL IPAA_SHIFL]] Rapidly associates with the first 265 amino acids of vinculin after bacteria-cell contact. This interaction is critical for efficient Shigella uptake. IpaA acts as a potent activator of vinculin and increase its ability to interact with F-actin. The complex IpaA-vinculin induces F-actin depolymerization along with the occasional formation of actin filament bundles.<ref>PMID:9184218</ref> <ref>PMID:10545097</ref>
| + | [https://www.uniprot.org/uniprot/VINC_CHICK VINC_CHICK] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:15229287</ref> <ref>PMID:20584916</ref> <ref>PMID:20086044</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Shigella paradysenteriae weldin 1927]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Chick]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Broos, J]] | |
| - | [[Category: Dijkstra, B W]] | |
| - | [[Category: Eerde, A van]] | |
| - | [[Category: Hamiaux, C]] | |
| - | [[Category: Parsot, C]] | |
| - | [[Category: Cell invasion]] | |
| - | [[Category: Helical bundle conversion]] | |
| - | [[Category: Ipaa-vinculin complex]] | |
| | [[Category: Shigella flexneri]] | | [[Category: Shigella flexneri]] |
| | + | [[Category: Broos J]] |
| | + | [[Category: Dijkstra BW]] |
| | + | [[Category: Hamiaux C]] |
| | + | [[Category: Parsot C]] |
| | + | [[Category: Van Eerde A]] |
| Structural highlights
Function
VINC_CHICK Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Invasion of epithelial cells by Shigella flexneri is characterized by cytoskeletal rearrangements of the host cell membrane, promoting internalization of the bacterium. The bacterial effector IpaA is injected into the epithelial cell by a type III secretion apparatus and recruits vinculin to regulate actin polymerization at the site of entry. We analysed the complex formed between a carboxy-terminal fragment of IpaA (IpaA(560-633)) and the vinculin D1 domain (VD1), both in crystals and in solution. We present evidence that IpaA(560-633) has two alpha-helical vinculin-binding sites that simultaneously bind two VD1 molecules. The interaction of IpaA(560-633) with VD1 is highly similar to the interaction of the endogenous, eukaryotic proteins talin and alpha-actinin with VD1, showing that Shigella uses a structural mimicry strategy to activate vinculin.
Structural mimicry for vinculin activation by IpaA, a virulence factor of Shigella flexneri.,Hamiaux C, van Eerde A, Parsot C, Broos J, Dijkstra BW EMBO Rep. 2006 Aug;7(8):794-9. Epub 2006 Jul 7. PMID:16826238[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang Z, Izaguirre G, Lin SY, Lee HY, Schaefer E, Haimovich B. The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading. Mol Biol Cell. 2004 Sep;15(9):4234-47. Epub 2004 Jun 30. PMID:15229287 doi:10.1091/mbc.E04-03-0264
- ↑ le Duc Q, Shi Q, Blonk I, Sonnenberg A, Wang N, Leckband D, de Rooij J. Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. J Cell Biol. 2010 Jun 28;189(7):1107-15. doi: 10.1083/jcb.201001149. PMID:20584916 doi:10.1083/jcb.201001149
- ↑ Peng X, Cuff LE, Lawton CD, DeMali KA. Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin. J Cell Sci. 2010 Feb 15;123(Pt 4):567-77. doi: 10.1242/jcs.056432. Epub 2010 Jan , 19. PMID:20086044 doi:10.1242/jcs.056432
- ↑ Hamiaux C, van Eerde A, Parsot C, Broos J, Dijkstra BW. Structural mimicry for vinculin activation by IpaA, a virulence factor of Shigella flexneri. EMBO Rep. 2006 Aug;7(8):794-9. Epub 2006 Jul 7. PMID:16826238
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