3D Model of Human TRMT5
(A) Ribbon presentation of the Methanocaldococcus jannaschii aTrm5–tRNACys(GCA)–AdoMet complex structure. The fragment of structure typical for the AdoMet-dependent methyltransferases superfamily (SCOP: SSF53335) is colored gray (the remaining portion of aTrm5 is colored cyan). tRNACys is colored light orange, and G37 is presented as a stick model. SAM are depicted as stick models and carbon atoms are yellow. The residues that are key for catalysis32 are indicated in green.
(B) Detailed view of the structural model of the catalytic site of aTrm5. Color coding is the same as in panel (A).
(C) Detailed view of the 3D model of the predicted catalytic site of human TRMT5. TRMT5 residues corresponding to the catalytically important amino acids in aTrm5 are indicated in dark green. Seven out of nine catalytically important residues are absolutely conserved in TRMT5 and aTrm5, and the remaining two, His289 (Methanocaldococcus jannaschii Arg186) and Arg454 (Methanocaldococcus jannaschii Lys318), share very similar chemical properties between the two proteins. The residues mutated in individuals 73901 and 65205, Arg291 and Met389, respectively, are indicated in red.