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PDBsum entry 2vs6
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References listed in PDB file
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Key reference
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Title
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The c-Terminal fragment of the ribosomal p protein complexed to trichosanthin reveals the interaction between the ribosome-Inactivating protein and the ribosome.
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Authors
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P.H.Too,
M.K.Ma,
A.N.Mak,
Y.T.Wong,
C.K.Tung,
G.Zhu,
S.W.Au,
K.B.Wong,
P.C.Shaw.
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Ref.
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Nucleic Acids Res, 2009,
37,
602-610.
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PubMed id
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Abstract
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Ribosome-inactivating proteins (RIPs) inhibit protein synthesis by enzymatically
depurinating a specific adenine residue at the sarcin-ricin loop of the 28S
rRNA, which thereby prevents the binding of elongation factors to the GTPase
activation centre of the ribosome. Here, we present the 2.2 A crystal structure
of trichosanthin (TCS) complexed to the peptide SDDDMGFGLFD, which corresponds
to the conserved C-terminal elongation factor binding domain of the ribosomal P
protein. The N-terminal region of this peptide interacts with Lys173, Arg174 and
Lys177 in TCS, while the C-terminal region is inserted into a hydrophobic
pocket. The interaction with the P protein contributes to the
ribosome-inactivating activity of TCS. This 11-mer C-terminal P peptide can be
docked with selected important plant and bacterial RIPs, indicating that a
similar interaction may also occur with other RIPs.
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