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PDBsum entry 6ofh
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Protein transport
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PDB id
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6ofh
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References listed in PDB file
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Key reference
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Title
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A polymorphic helix of a salmonella needle protein relays signals defining distinct steps in type III secretion.
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Authors
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E.Z.Guo,
D.C.Desrosiers,
J.Zalesak,
J.Tolchard,
M.Berbon,
B.Habenstein,
T.Marlovits,
A.Loquet,
J.E.Galán.
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Ref.
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PLoS Biol, 2019,
17,
e3000351.
[DOI no: ]
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PubMed id
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Abstract
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Type III protein-secretion machines are essential for the interactions of many
pathogenic or symbiotic bacterial species with their respective eukaryotic
hosts. The core component of these machines is the injectisome, a multiprotein
complex that mediates the selection of substrates, their passage through the
bacterial envelope, and ultimately their delivery into eukaryotic target cells.
The injectisome is composed of a large cytoplasmic complex or sorting platform,
a multiring base embedded in the bacterial envelope, and a needle-like filament
that protrudes several nanometers from the bacterial surface and is capped at
its distal end by the tip complex. A characteristic feature of these machines is
that their activity is stimulated by contact with target host cells. The sensing
of target cells, thought to be mediated by the distal tip of the needle
filament, generates an activating signal that must be transduced to the
secretion machine by the needle filament. Here, through a multidisciplinary
approach, including solid-state NMR (SSNMR) and cryo electron microscopy
(cryo-EM) analyses, we have identified critical residues of the needle filament
protein of a Salmonella Typhimurium type III secretion system that are involved
in the regulation of the activity of the secretion machine. We found that
mutations in the needle filament protein result in various specific phenotypes
associated with different steps in the type III secretion process. More
specifically, these studies reveal an important role for a polymorphic helix of
the needle filament protein and the residues that line the lumen of its central
channel in the control of type III secretion.
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