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Reassessment of MxiH subunit orientation and fold within native Shigella T3SS needles using surface labelling and solid-state NMR》.pdf

Reassessment of MxiH subunit orientation and fold within native Shigella T3SS needles using surface labelling and solid-state NMR》.pdf

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Reassessment of MxiH subunit orientation and fold within native Shigella T3SS needles using surface labelling and solid-state NMR》.pdf

Journal of Structural Biology xxx (2015) xxx–xxx Contents lists available at ScienceDirect Journal of Structural Biology journal homepage: www.else /locate/yjsbi Reassessment of MxiH subunit orientation and fold within native Shigella T3SS needles using surface labelling and solid-state NMR Joeri Verasdonck a,1, Da-Kang Shen b,1, Alexander Treadgold b,1, Christopher Arthur c, Anja Böckmann d,⇑, Beat H. Meier a,⇑, Ariel J. Blocker e,⇑ a Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland b School of Cellular Molecular Medicine, University of Bristol, BS8 1TD Bristol, United Kingdom c School of Chemistry, University of Bristol, BS8 1TS Bristol, United Kingdom d Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, Lyon, France e Schools of Cellular Molecular Medicine and Biochemistry, University of Bristol, BS8 1TD Bristol, United Kingdom a r t i c l e i n f o a b s t r a c t Article history: T3SSs are essential virulence determinants of many Gram-negative bacteria, used to inject bacterial effec- Received 20 July 2015 tors of virulence into eukaryotic host cells. Their major extracellular portion, a 50 nm hollow, needle- Received in revised form 29 September 2015 like structure, is essential to host cell sensing and the conduit for effector secretion. It is formed of a small, Accepted 2 October 2015 conserved subunit arranged as a helical polymer. The structure of the subunit has been studied by elec- Available online xxxx

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