Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex

Hyunmin Kim, Tomoko Kubori, Kohei Yamazaki, Mi-Jeong Kwak, Suk-Youl Park, Hiroki Nagai, Joseph P. Vogel and Byung-Ha Oh ()
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Hyunmin Kim: Korea Advanced Institute of Science and Technology
Tomoko Kubori: Gifu University
Kohei Yamazaki: Gifu University
Mi-Jeong Kwak: Korea Advanced Institute of Science and Technology
Suk-Youl Park: POSTECH
Hiroki Nagai: Gifu University
Joseph P. Vogel: Washington University School of Medicine
Byung-Ha Oh: Korea Advanced Institute of Science and Technology

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: Abstract The Legionella pneumophila Dot/Icm type IVB secretion system (T4BSS) is extremely versatile, translocating ~300 effector proteins into host cells. This specialized secretion system employs the Dot/Icm type IVB coupling protein (T4CP) complex, which includes IcmS, IcmW and LvgA, that are known to selectively assist the export of a subclass of effectors. Herein, the crystal structure of a four-subunit T4CP subcomplex bound to the effector protein VpdB reveals an interaction between LvgA and a linear motif in the C-terminus of VpdB. The same binding interface of LvgA also interacts with the C-terminal region of three additional effectors, SidH, SetA and PieA. Mutational analyses identified a FxxxLxxxK binding motif that is shared by VpdB and SidH, but not by SetA and PieA, showing that LvgA recognizes more than one type of binding motif. Together, this work provides a structural basis for how the Dot/Icm T4CP complex recognizes effectors, and highlights the multiple substrate-binding specificities of its adaptor subunit.

Date: 2020
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DOI: 10.1038/s41467-020-16397-0

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