Structural insights into the interaction of the ribosomal P stalk protein P2 with a type II ribosome-inactivating protein ricin.

ABSTRACT: Ricin is a type II ribosome-inactivating protein (RIP) that depurinates A⁴³²⁴ at the sarcin-ricin loop of 28 S ribosomal RNA (rRNA), thus inactivating the ribosome by preventing elongation factors from binding to the GTPase activation centre. Recent studies have disclosed that the conserved C-terminal domain (CTD) of eukaryotic ribosomal P stalk proteins is involved in the process that RIPs target ribosome. However, the details of the molecular interaction between ricin and P stalk proteins remain unknown. Here, we report the structure of ricin-A chain (RTA) in a complex with the CTD of the human ribosomal protein P2. The structure shows that the Phe¹¹¹, Leu¹¹³ and Phe¹¹⁴ residues of P2 insert into a hydrophobic pocket formed by the Tyr^183</

SUBMITTER: Fan X 

PROVIDER: S-EPMC5122897 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature