 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](ek5035fig1mag.jpg)
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Figure 1
(a) The crystal structure of D. melanogaster TRMT2A RRM, fragment 57–137, at 1.6 Å resolution. The structure is shown as a ribbon coloured according to the labelled secondary-structure elements. (b) The superposition of dmTRMT2A (PDB entry 7pv5, shown as a red ribbon) and hsTRMT2A RRM (PDB entry 7nto, shown as a navy blue ribbon). The putative and conserved RNA-binding residues are depicted. The sequence alignment below shows the positions of the consensus RNA-binding platforms RNP1 and RNP2 in human and fly TRMT2A. Conserved RNA-binding residues at positions 3 and 5 of RNP1 and position 2 of RNP2 are indicated in magenta. (c) A 2Fo − Fc electron-density map contoured at 1σ is shown for the modified Cys103 residues. After soaking the crystals with NaAuCl4, the cysteine residue was chemically modified at its S atom with two AuCl moieties. (d) Superposition of the dmTRMT2A RRM domain (PDB entry 7pv5, shown as a grey cartoon) with its homologous RRM structures in complex with nucleic acids as identified by the PDBeFold search. The amino-acid residues in the dmTRMT2A RRM domain indicated in (b) are shown as blue sticks. For clarity, only nucleic acids are shown (as yellow cartoons and orange sticks) in the overlapped homologous structures. The following structures were used for the in silico analysis: human U1 small nuclear ribonucleoprotein A with glmS ribozyme derived from B. anthracis (PDB entry 3l3c; Cochrane et al., 2009  ), the Sex-lethal (Sxl) protein of D. melanogaster in complex with ssRNA (PDB entry 1b7f; Handa et al., 1999), the C-terminal RRM2 domain of mouse TDP-43 in complex with single-stranded DNA (PDB entry 3d2w; Kuo et al., 2009), human TDP-43 RRM1–DNA complex (PDB entry 4iuf; Kuo et al., 2014) and Caenorhabditis elegans MEC-8 C-terminal RRM domain bound to AGCACA (PDB entry 6dg0; H. Soufari & C. D. Mackereth, unpublished work). |
![[Figure 1]](ek5035fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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