Structure of Trm7-Trm734 and Interaction Model between Trm7-Trm734 and Substrate tRNA (IMAGE)

Ehime University

Structure of Trm7-Trm734 and Interaction Model between Trm7-Trm734 and Substrate tRNA

Caption

(A) Trm7 (red) possesses a Rossmann fold catalytic domain. Trm734 is composed of three WD40 b-propeller domains [BPA (green), BPB (Blue) and BPC (yellow)]. Trm7 is captured by two WD40 b-propeller domains. This interaction has not been observed in other WD40 b-propeller domain proteins. (B) The molecular shape (blue net) of Trm7-Trm734 was calculated from the data of small angle X-ray scattering and was coincided with the crystal structure of Trm7-Trm734, showing that Trm7-Trm734 exists as a hetero-dimer in solution. (C) An electrostatic potential surface map is generated based on the crystal structure of Trm7-Trm734. The positively-charged areas are indicated in blue. These positively-charged areas are expected to be tRNA binding sites. When the D-arm region in substrate tRNA is placed onto the positively-charged area of BPB, the methylation site (ribose of G34) and two important residues (Cm32 and m1G37) are able to be placed onto Trm7. This model suggests that Trm734 is required for positioning of tRNA for methylation.

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Ehime University

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