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Nucleic Acids Research Advance Access originally published online on December 10, 2008
Nucleic Acids Research 2009 37(2):602-610; doi:10.1093/nar/gkn922
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Nucleic Acids Research, 2009, Vol. 37, No. 2 602-610
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

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

Priscilla Hiu-Mei Too1, Meiji Kit-Wan Ma1, Amanda Nga-Sze Mak1, Yuen-Ting Wong1, Christine Kit-Ching Tung1, Guang Zhu2, Shannon Wing-Ngor Au1, Kam-Bo Wong1 and Pang-Chui Shaw1,*

1Department of Biochemistry, Centre for Protein Science and Crystallography and Molecular Biotechnology Programme, The Chinese University of Hong Kong, Shatin, N.T. and 2Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China

*To whom correspondence should be addressed. Tel: +852 2609 6803; Fax: +852 2603 7246; Email: pcshaw{at}cuhk.edu.hk

Correspondence may also be addressed to Kam-Bo Wong. Tel: +852 2609 8024; Fax: +852 2603 7732; Email: kbwong{at}cuhk.edu.hk

Received June 6, 2008. Revised October 27, 2008. Accepted November 3, 2008.

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.


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