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==Shigella IpaA-VBS3/TBS in complex with the Talin VBS1 domain 488-512== | ==Shigella IpaA-VBS3/TBS in complex with the Talin VBS1 domain 488-512== | ||
<StructureSection load='5nl1' size='340' side='right' caption='[[5nl1]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='5nl1' size='340' side='right'caption='[[5nl1]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nl1]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NL1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5nl1]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NL1 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tln1, Tln ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), ipaA, CP0125 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nl1 OCA], [http://pdbe.org/5nl1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nl1 RCSB], [http://www.ebi.ac.uk/pdbsum/5nl1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nl1 ProSAT]</span></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=5nl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nl1 OCA], [http://pdbe.org/5nl1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nl1 RCSB], [http://www.ebi.ac.uk/pdbsum/5nl1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nl1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TLN1_MOUSE TLN1_MOUSE]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. [[http://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> | [[http://www.uniprot.org/uniprot/TLN1_MOUSE TLN1_MOUSE]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. [[http://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> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Shigella type III effector IpaA contains three binding sites for the focal adhesion protein vinculin (VBSs), which are involved in bacterial invasion of host cells. Here, we report that IpaA VBS3 unexpectedly binds to talin. The 2.5 A resolution crystal structure of IpaA VBS3 in complex with the talin H1-H4 helices shows a tightly folded alpha-helical bundle, which is in contrast to the bundle unraveling upon vinculin interaction. High-affinity binding to talin H1-H4 requires a core of hydrophobic residues and electrostatic interactions conserved in talin VBS H46. Remarkably, IpaA VBS3 localizes to filopodial distal adhesions enriched in talin, but not vinculin. In addition, IpaA VBS3 binding to talin was required for filopodial adhesions and efficient capture of Shigella. These results point to the functional diversity of VBSs and support a specific role for talin binding by a subset of VBSs in the formation of filopodial adhesions. | |||
Shigella IpaA Binding to Talin Stimulates Filopodial Capture and Cell Adhesion.,Valencia-Gallardo C, Bou-Nader C, Aguilar-Salvador DI, Carayol N, Quenech'Du N, Pecqueur L, Park H, Fontecave M, Izard T, Tran Van Nhieu G Cell Rep. 2019 Jan 22;26(4):921-932.e6. doi: 10.1016/j.celrep.2018.12.091. PMID:30673614<ref>PMID:30673614</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5nl1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Talin|Talin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Shigella paradysenteriae weldin 1927]] | |||
[[Category: Large Structures]] | |||
[[Category: Lk3 transgenic mice]] | |||
[[Category: Bou-Nader, C]] | [[Category: Bou-Nader, C]] | ||
[[Category: Fontecave, M]] | [[Category: Fontecave, M]] | ||
Revision as of 10:22, 23 May 2019
Shigella IpaA-VBS3/TBS in complex with the Talin VBS1 domain 488-512Shigella IpaA-VBS3/TBS in complex with the Talin VBS1 domain 488-512
Structural highlights
Function[TLN1_MOUSE] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. [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.[1] [2] Publication Abstract from PubMedThe Shigella type III effector IpaA contains three binding sites for the focal adhesion protein vinculin (VBSs), which are involved in bacterial invasion of host cells. Here, we report that IpaA VBS3 unexpectedly binds to talin. The 2.5 A resolution crystal structure of IpaA VBS3 in complex with the talin H1-H4 helices shows a tightly folded alpha-helical bundle, which is in contrast to the bundle unraveling upon vinculin interaction. High-affinity binding to talin H1-H4 requires a core of hydrophobic residues and electrostatic interactions conserved in talin VBS H46. Remarkably, IpaA VBS3 localizes to filopodial distal adhesions enriched in talin, but not vinculin. In addition, IpaA VBS3 binding to talin was required for filopodial adhesions and efficient capture of Shigella. These results point to the functional diversity of VBSs and support a specific role for talin binding by a subset of VBSs in the formation of filopodial adhesions. Shigella IpaA Binding to Talin Stimulates Filopodial Capture and Cell Adhesion.,Valencia-Gallardo C, Bou-Nader C, Aguilar-Salvador DI, Carayol N, Quenech'Du N, Pecqueur L, Park H, Fontecave M, Izard T, Tran Van Nhieu G Cell Rep. 2019 Jan 22;26(4):921-932.e6. doi: 10.1016/j.celrep.2018.12.091. PMID:30673614[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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