4GC9
Crystal structure of murine TFB1M in complex with SAM
4GC9 の概要
| エントリーDOI | 10.2210/pdb4gc9/pdb |
| 関連するPDBエントリー | 4GC5 |
| 分子名称 | Dimethyladenosine transferase 1, mitochondrial, S-ADENOSYLMETHIONINE, ACETATE ION, ... (4 entities in total) |
| 機能のキーワード | methyltransferase fold, rrna methyltransferase, s-adenosyl-l-methionine, methylation, mitochondria, transferase |
| 由来する生物種 | Mus musculus (mouse) |
| 細胞内の位置 | Mitochondrion (By similarity): Q8JZM0 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 39805.34 |
| 構造登録者 | Guja, K.E.,Yakubovskaya, E.,Shi, H.,Mejia, E.,Hambardjieva, E.,Venkataraman, K.,Karzai, A.W.,Garcia-Diaz, M. (登録日: 2012-07-30, 公開日: 2013-07-10, 最終更新日: 2024-11-20) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.103 Å) |
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