Backbone and side-chain chemical shift assignments for the ribosome-inactivating protein trichobakin (TBK)

Autor: Vladimir V. Britikov, Dmitry M. Lesovoy, Anatoly S. Urban, Thi Bich Thao Le, Eduard V. Bocharov, Alexander S. Arseniev, Elena V. Britikova, Sergey A. Usanov, Chi Van Phan
Rok vydání: 2019
Předmět:
Zdroj: Biomolecular NMR Assignments. 14:55-61
ISSN: 1874-270X
1874-2718
Popis: Trichobakin (TBK) is a type-I ribosome-inactivating protein (RIP-I), acting as an extremely potent inhibitor of protein synthesis in the cell-free translation system of rabbit reticulocyte lysate (IC50: 3.5 pM). In this respect, TBK surpasses the well-studied highly homologous RIP-I trichosanthin (IC50: 20-27 pM), therefore creation of recombinant toxins based on it is of great interest. TBK needs to penetrate into cytosol through the cell membrane and specifically bind to α-sarcin/ricin loop of 28S ribosome RNA to perform the function of specific RNA depurination. At the moment, there is no detailed structural-dynamic information in solution about diverse states RIP-I can adopt at different stages on the way to protein synthesis inhibition. In this work, we report a near-complete assignment of 1H, 13C, and 15N TBK (27.3 kDa) resonances and analysis of the secondary structure based on the experimental chemical shifts data. This work will serve as a basis for further investigations of the structure, dynamics and interactions of the TBK with its molecular partners using NMR techniques.
Databáze: OpenAIRE
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