C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome

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 Å crys...

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Published in:Nucleic acids research 2009-02, Vol.37 (2), p.602-610
Main Authors: Too, Priscilla Hiu-Mei, Ma, Meiji Kit-Wan, Mak, Amanda Nga-Sze, Wong, Yuen-Ting, Tung, Christine Kit-Ching, Zhu, Guang, Au, Shannon Wing-Ngor, Wong, Kam-Bo, Shaw, Pang-Chui
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Models, Molecular
Molecular Sequence Data
Peptides - chemistry
Phosphoproteins - chemistry
Protein Structure, Tertiary
Ribosomal Proteins - chemistry
Sequence Homology, Amino Acid
Structural Biology
Trichosanthin - chemistry
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Summary: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 Å 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.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkn922