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PDBsum entry 4q5e
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Unknown function, protein binding
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PDB id
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4q5e
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Contents |
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168 a.a.
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76 a.a.
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155 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural basis for the inhibition of host protein ubiquitination by shigella effector kinase ospg.
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Authors
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A.M.Grishin,
T.E.Condos,
K.R.Barber,
F.X.Campbell-Valois,
C.Parsot,
G.S.Shaw,
M.Cygler.
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Ref.
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Structure, 2014,
22,
878-888.
[DOI no: ]
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PubMed id
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Abstract
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Shigella invasion of its human host is assisted by T3SS-delivered effector
proteins. The OspG effector kinase binds ubiquitin and ubiquitin-loaded
E2-conjugating enzymes, including UbcH5b and UbcH7, and attenuates the host
innate immune NF-kB signaling. We present the structure of OspG bound to the
UbcH7∼Ub conjugate. OspG has a minimal kinase fold lacking the activation loop
of regulatory kinases. UbcH7∼Ub binds OspG at sites remote from the kinase
active site, yet increases its kinase activity. The ubiquitin is positioned in
the "open" conformation with respect to UbcH7 using its I44 patch to
interact with the C terminus of OspG. UbcH7 binds to OspG using two conserved
loops essential for E3 ligase recruitment. The interaction of the UbcH7∼Ub
with OspG is remarkably similar to the interaction of an E2∼Ub with a HECT E3
ligase. OspG interferes with the interaction of UbcH7 with the E3 parkin and
inhibits the activity of the E3.
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