한빛사 논문
Hyunmin Kim1, Tomoko Kubori2, Kohei Yamazaki2,5, Mi-Jeong Kwak1,6, Suk-Youl Park3, Hiroki Nagai2, Joseph P. Vogel4 & Byung-Ha Oh1,*
1Department of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.
2Department of Microbiology, Graduate School of Medicine, Gifu University, 1-1 Yanagido, Gifu 501-1194, Japan.
3Pohang Accelerator Laboratory, POSTECH, Pohang, Gyeongbuk 37673, Republic of Korea.
4Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
5Present address: Veterinary Public Health, Kitasato University, Higashi 23-35-1, Towada, Aomori 034-8628, Japan.
6Present address: CKD Research Institute, Yongin, Gyeonggi 16995, Republic of Korea.
*Corresponding author
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.
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