4GC9
Crystal structure of murine TFB1M in complex with SAM
Summary for 4GC9
| Entry DOI | 10.2210/pdb4gc9/pdb |
| Related | 4GC5 |
| Descriptor | Dimethyladenosine transferase 1, mitochondrial, S-ADENOSYLMETHIONINE, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | methyltransferase fold, rrna methyltransferase, s-adenosyl-l-methionine, methylation, mitochondria, transferase |
| Biological source | Mus musculus (mouse) |
| Cellular location | Mitochondrion (By similarity): Q8JZM0 |
| Total number of polymer chains | 1 |
| Total formula weight | 39805.34 |
| Authors | Guja, K.E.,Yakubovskaya, E.,Shi, H.,Mejia, E.,Hambardjieva, E.,Venkataraman, K.,Karzai, A.W.,Garcia-Diaz, M. (deposition date: 2012-07-30, release date: 2013-07-10, Last modification date: 2023-12-06) |
| Primary citation | Guja, K.E.,Venkataraman, K.,Yakubovskaya, E.,Shi, H.,Mejia, E.,Hambardjieva, E.,Karzai, A.W.,Garcia-Diaz, M. Structural basis for S-adenosylmethionine binding and methyltransferase activity by mitochondrial transcription factor B1. Nucleic Acids Res., 41:7947-7959, 2013 Cited by PubMed Abstract: Eukaryotic transcription factor B (TFB) proteins are homologous to KsgA/Dim1 ribosomal RNA (rRNA) methyltransferases. The mammalian TFB1, mitochondrial (TFB1M) factor is an essential protein necessary for mitochondrial gene expression. TFB1M mediates an rRNA modification in the small ribosomal subunit and thus plays a role analogous to KsgA/Dim1 proteins. This modification has been linked to mitochondrial dysfunctions leading to maternally inherited deafness, aminoglycoside sensitivity and diabetes. Here, we present the first structural characterization of the mammalian TFB1 factor. We have solved two X-ray crystallographic structures of TFB1M with (2.1 Å) and without (2.0 Å) its cofactor S-adenosyl-L-methionine. These structures reveal that TFB1M shares a conserved methyltransferase core with other KsgA/Dim1 methyltransferases and shed light on the structural basis of S-adenosyl-L-methionine binding and methyltransferase activity. Together with mutagenesis studies, these data suggest a model for substrate binding and provide insight into the mechanism of methyl transfer, clarifying the role of this factor in an essential process for mitochondrial function. PubMed: 23804760DOI: 10.1093/nar/gkt547 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.103 Å) |
Structure validation
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