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Justin Porter

As seen in: Science Magazine
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The Yeh pilus adhesin is equipped with an α-helical flap motif, which contributes to pectin adherence

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By Janni Yuval, Xintao Li, Juha Aalto, Kevin Tamadonfar, Roger Klein, Maxwell I. Zimmerman, Philippe N. Azimzadeh, Denise Sanick, Justin Porter, Jesus Bazan Villicana, Jerome S. Pinkner, Nathaniel C. Gualberto, Karen W. Dodson, Bo Huey Chiang, Michael L. Patno
| Science Magazine
Abstract The Yeh chaperone-usher pathway (CUP) pilus adhesin is encoded in one-half of all Escherichia coli. Yet little is known about its structure and function in E. coli persistence and pathogenesis. Structural investigations reveal that the adhesin receptor binding domains (RBDs) of YehD and its relative YhlD both share a canonical β-rich core and an α-helical flap motif that is hinged at the distal end of the core.
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