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- Title
The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome.
- 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
- Abstract
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.
- Publication
Nucleic acids research, 2009, Vol 37, Issue 2, p602
- ISSN
1362-4962
- Publication type
Journal Article
- DOI
10.1093/nar/gkn922