2lnh

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==Enterohaemorrhagic E. coli (EHEC) exploits a tryptophan switch to hijack host F-actin assembly==
==Enterohaemorrhagic E. coli (EHEC) exploits a tryptophan switch to hijack host F-actin assembly==
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<StructureSection load='2lnh' size='340' side='right' caption='[[2lnh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2lnh' size='340' side='right'caption='[[2lnh]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2lnh]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LNH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2lnh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LNH FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WASL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), BAIAP2L1, IRTKS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), espF(U), tccP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 Escherichia coli O157:H7])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lnh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lnh RCSB], [http://www.ebi.ac.uk/pdbsum/2lnh PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lnh OCA], [https://pdbe.org/2lnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lnh RCSB], [https://www.ebi.ac.uk/pdbsum/2lnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lnh ProSAT]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/WASL_HUMAN WASL_HUMAN] Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression.<ref>PMID:19366662</ref>
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Intrinsically disordered protein (IDP)-mediated interactions are often characterized by low affinity but high specificity. These traits are essential in signaling and regulation that require reversibility. Enterohaemorrhagic Escherichia coli (EHEC) exploit this situation by commandeering host cytoskeletal signaling to stimulate actin assembly beneath bound bacteria, generating "pedestals" that promote intestinal colonization. EHEC translocates two proteins, EspF(U) and Tir, which form a complex with the host protein IRTKS. The interaction of this complex with N-WASP triggers localized actin polymerization. We show that EspF(U) is an IDP that contains a transiently alpha-helical N-terminus and dynamic C-terminus. Our structure shows that single EspF(U) repeat forms a high-affinity trimolecular complex with N-WASP and IRTKS. We demonstrate that bacterial and cellular ligands interact with IRTKS SH3 in a similar fashion, but the bacterial protein has evolved to outcompete cellular targets by utilizing a tryptophan switch that offers superior binding affinity enabling EHEC-induced pedestal formation.
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Enterohaemorrhagic Escherichia Coli Exploits a Tryptophan Switch to Hijack Host F-Actin Assembly.,Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P Structure. 2012 Aug 21. PMID:22921828<ref>PMID:22921828</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Wiskott-Aldrich syndrome protein 3D structures|Wiskott-Aldrich syndrome protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli o157:h7]]
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[[Category: Escherichia coli O157:H7]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Aitio, O.]]
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[[Category: Large Structures]]
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[[Category: Hellman, M.]]
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[[Category: Aitio O]]
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[[Category: Kesti, T.]]
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[[Category: Hellman M]]
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[[Category: Leong, J M.]]
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[[Category: Kesti T]]
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[[Category: Permi, P.]]
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[[Category: Leong JM]]
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[[Category: Saksela, K.]]
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[[Category: Permi P]]
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[[Category: Skehan, B.]]
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[[Category: Saksela K]]
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[[Category: Protein complex]]
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[[Category: Skehan B]]
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[[Category: Signaling protein-protein binding complex]]
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Current revision

Enterohaemorrhagic E. coli (EHEC) exploits a tryptophan switch to hijack host F-actin assembly

PDB ID 2lnh

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