Fig. 1: Structural insights into tRNA-Leu recognition, binding, and cleavage by SLFN11. | Nature Communications

Fig. 1: Structural insights into tRNA-Leu recognition, binding, and cleavage by SLFN11.

From: Phosphorylation-mediated conformational change regulates human SLFN11

Fig. 1

a Domain architecture of SLFN11 with indicated key functional features. b Cryo-EM density map for SLFN11 bound to tRNA-Leu (left). tRNA is colored in green with the variable arm highlighted in pink. The position of the inset f is highlighted. The map was postprocessed in cryoSPARC by DeepEMhancer44. Cartoon representation of SLFN11 bound to tRNA-Leu with highlighted structural features (right). tRNA-Leu is color-coded based on the scheme in c. The nuclease active sites of both SLFN11 protomers are indicated. c Schematic representation of type II tRNA-Leu. Structural features of the tRNA are labeled and color-coded. The SLFN11 cleavage site is indicated. d Bottom view of tRNA-Leu bound to the nuclease domains of the SLFN11 dimer. The nuclease active sites of both SLFN11 protomers are highlighted. e Close-up view on nuclease active site I (left) and II (right) with bound tRNA-Leu. The cleavage site of tRNA-Leu between position 76 and 77 is indicated in nuclease active site I. f Detailed view of the interaction of the nuclease ___domain of SLFN11 with the variable arm of tRNA-Leu. g Analysis of the endonucleolytic cleavage of tRNA-Leu and tRNA-Leu Δvar in a competitive tRNA-cleavage assay. Data are represented as mean values +/− SD from three independent experiments. Source data for g are provided as a Source Data file.

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