title: Structural basis of α-catenin recognition by EspB from enterohaemorrhagic E. coli based on hybrid strategy using low-resolution structural and protein dissection.
abstract: Enterohaemorrhagic E. coli (EHEC) induces actin reorganization of host cells by injecting various effectors into host cytosol through type III secretion systems. EspB is the natively partially folded EHEC effector which binds to host α-catenin to promote the actin bundling. However, its structural basis is poorly understood. Here, we characterize the overall structural properties of EspB based on low-resolution structural data in conjunction with protein dissection strategy. EspB showed a unique thermal response involving cold denaturation in the presence of denaturant according to far-UV circular dichroism (CD). Small angle X-ray scattering revealed the formation of a highly extended structure of EspB comparable to the ideal random coil. Various disorder predictions as well as CD spectra of EspB fragments identified the presence of α-helical structures around G41 to Q70. The fragment corresponding to this region indicated the thermal response similar to EspB. Moreover, this fragment showed a high affinity to C-terminal vinculin homology domain of α-catenin. The results clarified the importance of preformed α-helix of EspB for recognition of α-catenin.
authors: Department of Emergency Critical Care Medicine, School of Medicine, Kinki University, Osakasayama, Osaka, Japan.
authors: Mitsuhide
authors: M
authors: Hamaguchi
authors: Hironari
authors: H
authors: Kamikubo
authors: Kayo N
authors: KN
authors: Suzuki
authors: Yoshihisa
authors: Y
authors: Hagihara
authors: Itaru
authors: I
authors: Yanagihara
authors: Ikuhiro
authors: I
authors: Sakata
authors: Mikio
authors: M
authors: Kataoka
authors: Daizo
authors: D
authors: Hamada
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D002942:Circular Dichroism; D054324:Enterohemorrhagic Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary; D058767:Protein Unfolding; D053838:Scattering, Small Angle; D013816:Thermodynamics; D014961:X-Ray Diffraction; D051178:alpha Catenin / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001425:Bacterial Outer Membrane Proteins; C087863:EaeB protein, E coli; D029968:Escherichia coli Proteins; D051178:alpha Catenin
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