2zzm | pdb_00002zzm
The complex structure of aTrm5 and tRNALeu
Structural highlights
FunctionTRM5B_METJA Specifically methylates the N1 position of guanosine-37 in various tRNAs.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedtRNA precursors undergo a maturation process, involving nucleotide modifications and folding into the L-shaped tertiary structure. The N1-methylguanosine at position 37 (m1G37), 3' adjacent to the anticodon, is essential for translational fidelity and efficiency. In archaea and eukaryotes, Trm5 introduces the m1G37 modification into all tRNAs bearing G37. Here we report the crystal structures of archaeal Trm5 (aTrm5) in complex with tRNA(Leu) or tRNA(Cys). The D2-D3 domains of aTrm5 discover and modify G37, independently of the tRNA sequences. D1 is connected to D2-D3 through a flexible linker and is designed to recognize the shape of the tRNA outer corner, as a hallmark of the completed L shape formation. This interaction by D1 lowers the K(m) value for tRNA, enabling the D2-D3 catalysis. Thus, we propose that aTrm5 provides the tertiary structure checkpoint in tRNA maturation. Tertiary structure checkpoint at anticodon loop modification in tRNA functional maturation.,Goto-Ito S, Ito T, Kuratani M, Bessho Y, Yokoyama S Nat Struct Mol Biol. 2009 Oct;16(10):1109-15. Epub 2009 Sep 13. PMID:19749755[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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