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J Struct Biol. 2015 Dec;192(3):441-448. doi: 10.1016/j.jsb.2015.10.005. Epub 2015 Oct 6.

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

Author information

1
Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland.
2
School of Cellular & Molecular Medicine, University of Bristol, BS8 1TD Bristol, United Kingdom.
3
School of Chemistry, University of Bristol, BS8 1TS Bristol, United Kingdom.
4
Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, Lyon, France. Electronic address: a.bockmann@ibcp.fr.
5
Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland. Electronic address: beme@ethz.ch.
6
Schools of Cellular & Molecular Medicine and Biochemistry, University of Bristol, BS8 1TD Bristol, United Kingdom. Electronic address: ariel.blocker@bristol.ac.uk.

Abstract

T3SSs are essential virulence determinants of many Gram-negative bacteria, used to inject bacterial effectors of virulence into eukaryotic host cells. Their major extracellular portion, a ∼50 nm hollow, needle-like structure, is essential to host cell sensing and the conduit for effector secretion. It is formed of a small, conserved subunit arranged as a helical polymer. The structure of the subunit has been studied by electron cryomicroscopy within native polymers and by solid-state NMR in recombinant polymers, yielding two incompatible atomic models. To resolve this controversy, we re-examined the native polymer used for electron cryomicroscopy via surface labelling and solid-state NMR. Our data show the orientation and overall fold of the subunit within this polymer is as established by solid-state NMR for recombinant polymers.

KEYWORDS:

Needle; Shigella; Solid-state NMR; Surface labelling; Type III secretion

PMID:
26439285
PMCID:
PMC4658334
DOI:
10.1016/j.jsb.2015.10.005
[Indexed for MEDLINE]
Free PMC Article

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