2V3J
The yeast ribosome synthesis factor Emg1 alpha beta knot fold methyltransferase
Summary for 2V3J
| Entry DOI | 10.2210/pdb2v3j/pdb |
| Related | 2V3K |
| Descriptor | ESSENTIAL FOR MITOTIC GROWTH 1, SULFATE ION (3 entities in total) |
| Functional Keywords | emg1, rrna processing, nuclear protein, ribonucleoprotein, ribosome biogenesis, alpha/beta knot fold methyltransferase, ribosomal protein |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Total number of polymer chains | 1 |
| Total formula weight | 29238.83 |
| Authors | Leulliot, N.,Bohnsack, M.T.,Graille, M.,Tollervey, D.,Van Tilbeurgh, H. (deposition date: 2007-06-18, release date: 2007-12-04, Last modification date: 2024-10-16) |
| Primary citation | Leulliot, N.,Bohnsack, M.T.,Graille, M.,Tollervey, D.,Van Tilbeurgh, H. The Yeast Ribosome Synthesis Factor Emg1 is a Novel Member of the Superfamily of Alpha/Beta Knot Fold Methyltransferases. Nucleic Acids Res., 36:629-, 2008 Cited by PubMed Abstract: Emg1 was previously shown to be required for maturation of the 18S rRNA and biogenesis of the 40S ribosomal subunit. Here we report the determination of the crystal structure of Emg1 at 2 A resolution in complex with the methyl donor, S-adenosyl-methionine (SAM). This structure identifies Emg1 as a novel member of the alpha/beta knot fold methyltransferase (SPOUT) superfamily. In addition to the conserved SPOUT core, Emg1 has two unique domains that form an extended surface, which we predict to be involved in binding of RNA substrates. A point mutation within a basic patch on this surface almost completely abolished RNA binding in vitro. Three point mutations designed to disrupt the interaction of Emg1 with SAM each caused>100-fold reduction in SAM binding in vitro. Expression of only Emg1 with these mutations could support growth and apparently normal ribosome biogenesis in strains genetically depleted of Emg1. We conclude that the catalytic activity of Emg1 is not essential and that the presence of the protein is both necessary and sufficient for ribosome biogenesis. PubMed: 18063569DOI: 10.1093/NAR/GKM1074 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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