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PDBsum entry 3wkl
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DOI no:
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Structure
22:326-336
(2014)
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PubMed id:
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A structure-based model of substrate discrimination by a noncanonical PDZ tandem in the intramembrane-cleaving protease RseP.
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Y.Hizukuri,
T.Oda,
S.Tabata,
K.Tamura-Kawakami,
R.Oi,
M.Sato,
J.Takagi,
Y.Akiyama,
T.Nogi.
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ABSTRACT
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During the extracytoplasmic stress response in Escherichia coli, the
intramembrane protease RseP cleaves the anti-σ(E) protein RseA only after the
membrane-anchored protease DegS truncates the periplasmic part of RseA that
suppresses the action of RseP. Here we analyzed the three-dimensional structure
of the two tandemly arranged PSD-95/Dlg/ZO-1 (PDZ) domains (PDZ tandem) present
in the periplasmic region of RseP and revealed that the two putative
ligand-binding grooves constitute a single pocket-like structure that would lie
just above the active center sequestrated within the membrane. Complete removal
of the PDZ tandem from RseP led to the intramembrane cleavage of RseA without
prior truncation by DegS. Furthermore, mutations expected to destabilize the
tertiary structure of the PDZ tandem also caused the deregulation of the
sequential cleavage. These observations suggest that the PDZ tandem serves as a
size-exclusion filter to accommodate the truncated form of RseA into the active
center.
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');
}
}
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