6H2V
Crystal structure of human METTL5-TRMT112 complex, the 18S rRNA m6A1832 methyltransferase at 2.5A resolution
Summary for 6H2V
| Entry DOI | 10.2210/pdb6h2v/pdb |
| Descriptor | Methyltransferase-like protein 5, Multifunctional methyltransferase subunit TRM112-like protein, S-ADENOSYLMETHIONINE, ... (8 entities in total) |
| Functional Keywords | rrna maturation, methyltransferase, translation, ribosome synthesis, transferase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 79685.67 |
| Authors | van Tran, N.,Graille, M. (deposition date: 2018-07-16, release date: 2019-07-31, Last modification date: 2024-11-06) |
| Primary citation | van Tran, N.,Ernst, F.G.M.,Hawley, B.R.,Zorbas, C.,Ulryck, N.,Hackert, P.,Bohnsack, K.E.,Bohnsack, M.T.,Jaffrey, S.R.,Graille, M.,Lafontaine, D.L.J. The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112. Nucleic Acids Res., 47:7719-7733, 2019 Cited by PubMed Abstract: N6-methyladenosine (m6A) has recently been found abundantly on messenger RNA and shown to regulate most steps of mRNA metabolism. Several important m6A methyltransferases have been described functionally and structurally, but the enzymes responsible for installing one m6A residue on each subunit of human ribosomes at functionally important sites have eluded identification for over 30 years. Here, we identify METTL5 as the enzyme responsible for 18S rRNA m6A modification and confirm ZCCHC4 as the 28S rRNA modification enzyme. We show that METTL5 must form a heterodimeric complex with TRMT112, a known methyltransferase activator, to gain metabolic stability in cells. We provide the first atomic resolution structure of METTL5-TRMT112, supporting that its RNA-binding mode differs distinctly from that of other m6A RNA methyltransferases. On the basis of similarities with a DNA methyltransferase, we propose that METTL5-TRMT112 acts by extruding the adenosine to be modified from a double-stranded nucleic acid. PubMed: 31328227DOI: 10.1093/nar/gkz619 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
Download full validation report
