2VS6

K173A, R174A, K177A-trichosanthin

Summary for 2VS6

• Entry DOI: 10.2210/pdb2vs6/pdb
• Related: 1GIS 1GIU 1J4G 1MRJ 1MRK 1NLI 1QD2 1TCS 2JDL 2JJR
• Descriptor: RIBOSOME-INACTIVATING PROTEIN ALPHA-TRICHOSANTHIN (2 entities in total)
• Functional Keywords: antiviral protein, protein synthesis inhibitor, tcs, toxin, hydrolase, plant defense
• Biological source: TRICHOSANTHES KIRILOWII (MONGOLIAN SNAKE-GOURD)
• Total number of polymer chains: 2
• Total formula weight: 54191.29

Authors

Too, P.H.,Ma, M.K.,Mak, A.N.,Tung, C.K.,Zhu, G.,Au, S.W.,Wong, K.B.,Shaw, P.C.,Ng, A. (deposition date: 2008-04-21, release date: 2008-12-30, Last modification date: 2023-12-13)

Primary citation

Too, P.H.,Ma, M.K.,Mak, A.N.,Wong, Y.T.,Tung, C.K.,Zhu, G.,Au, S.W.,Wong, K.B.,Shaw, P.C.
The C-Terminal Fragment of the Ribosomal P Protein Complexed to Trichosanthin Reveals the Interaction between the Ribosome-Inactivating Protein and the Ribosome.
Nucleic Acids Res., 37:602-, 2009

PubMed 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.

PubMed: 19073700
DOI: 10.1093/NAR/GKN922

Experimental method

X-RAY DIFFRACTION (2.4 Å)