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PDBsum entry 4c2f
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References listed in PDB file
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Key reference
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Title
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Ctpb assembles a gated protease tunnel regulating cell-Cell signaling during spore formation in bacillus subtilis.
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Authors
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M.Mastny,
A.Heuck,
R.Kurzbauer,
A.Heiduk,
P.Boisguerin,
R.Volkmer,
M.Ehrmann,
C.D.Rodrigues,
D.Z.Rudner,
T.Clausen.
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Ref.
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Cell, 2013,
155,
647-658.
[DOI no: ]
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PubMed id
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Abstract
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Spore formation in Bacillus subtilis relies on a regulated intramembrane
proteolysis (RIP) pathway that synchronizes mother-cell and forespore
development. To address the molecular basis of this SpoIV transmembrane
signaling, we carried out a structure-function analysis of the activating
protease CtpB. Crystal structures reflecting distinct functional states show
that CtpB constitutes a ring-like protein scaffold penetrated by two narrow
tunnels. Access to the proteolytic sites sequestered within these tunnels is
controlled by PDZ domains that rearrange upon substrate binding. Accordingly,
CtpB resembles a minimal version of a self-compartmentalizing protease regulated
by a unique allosteric mechanism. Moreover, biochemical analysis of the
PDZ-gated channel combined with sporulation assays reveal that activation of the
SpoIV RIP pathway is induced by the concerted activity of CtpB and a second
signaling protease, SpoIVB. This proteolytic mechanism is of broad relevance for
cell-cell communication, illustrating how distinct signaling pathways can be
integrated into a single RIP module.
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