Fig. 4: Structure of METTL15 in complex with RNA, hsRBFA226–260 and SFG. | Cell Discovery

Fig. 4: Structure of METTL15 in complex with RNA, hsRBFA226–260 and SFG.

From: Structural insights into the specific recognition of mitochondrial ribosome-binding factor hsRBFA and 12 S rRNA by methyltransferase METTL15

Fig. 4: Structure of METTL15 in complex with RNA, hsRBFA226–260 and SFG.The alternative text for this image may have been generated using AI.

a Cartoon representation of the METTL1570–407–RNA–hsRBFA226–260–SFG quaternary complex in two orientations related by a 180° rotation around a vertical axis. The asymmetric unit consisted of the METTL15 (cyan), h44_dsRNA1 (slate), hsRBFA (bright orange) and SFG (magenta). In the left pannel, the MTases domain (domain 1) is colored in cyan and the scaffold-like domain (domain 2) in slate, respectively. b The binding affinities of 5’-FAM-labeled RNAs for METTL15 determined by FP experiments are shown. c The RNA and C-terminal helix of hsRBFA are represented as sticks binding to the either side of METTL15, respectively. The positively charged, negatively charged and neutral areas are represented in blue, red and white, respectively. d Higher magnification views of individual interactions between METTL15 (cyan, labeled blue) and h44_dsRNA1 (slate). Hydrogen bonds are indicated with yellow dotted lines. e Superposition of the METTL1570–407–RNA–hsRBFA226–260–SFG quaternary complex with the cryo-electron structure of pre-mt-SSU (PDB ID 7PNX). The METTL1570–407–RNA–hsRBFA226–260–SFG quaternary complex colored as described in (a), except the h44_dsRNA1 colored red. The METTL15 and hsRBFA in pre-mt-SSU are colored magenta and light pink, respectively.

Back to article page