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PDBsum entry 2lnh
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Signaling protein/protein binding
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PDB id
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2lnh
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References listed in PDB file
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Key reference
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Title
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Enterohaemorrhagic escherichia coli exploits a tryptophan switch to hijack host f-Actin assembly.
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Authors
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O.Aitio,
M.Hellman,
B.Skehan,
T.Kesti,
J.M.Leong,
K.Saksela,
P.Permi.
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Ref.
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Structure, 2012,
20,
1692-1703.
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PubMed id
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Abstract
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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
α-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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