Fig. 3: Structure of METTL15 in complex with hsRBFA226–260 and SAM. | Cell Discovery

Fig. 3: Structure of METTL15 in complex with hsRBFA226–260 and SAM.

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

Fig. 3: Structure of METTL15 in complex with hsRBFA226–260 and SAM.The alternative text for this image may have been generated using AI.

a Cartoon representation of the METTL1570–407–hsRBFA226–260–SAM ternary complex in two orientations related by a 180° rotation around a vertical axis. The asymmetric unit consists of the METTL15 (cyan), hsRBFA (bright orange) and SAM (magenta). b Schematic of hsRBFA interactions with METTL15, colored as described in (a). The red and black dotted lines indicate contacts mediated by hydrogen bonds and water-bridged hydrogen bonds, respectively. c The C-terminal helix of hsRBFA are represented as sticks on the molecular face of METTL15. 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 hsRBFA (bright orange, labeled black). Hydrogen bonds are indicated with black dotted lines.

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