6IRV
Crystal structure of the human cap-specific adenosine methyltransferase
Summary for 6IRV
| Entry DOI | 10.2210/pdb6irv/pdb |
| Descriptor | Phosphorylated CTD-interacting factor 1 (2 entities in total) |
| Functional Keywords | rna methylation, methyltransferase, m6a, n6-methyladenosine, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 118786.05 |
| Authors | Hirano, S.,Nishimasu, H.,Ishitani, R.,Nureki, O. (deposition date: 2018-11-14, release date: 2018-12-05, Last modification date: 2023-11-22) |
| Primary citation | Akichika, S.,Hirano, S.,Shichino, Y.,Suzuki, T.,Nishimasu, H.,Ishitani, R.,Sugita, A.,Hirose, Y.,Iwasaki, S.,Nureki, O.,Suzuki, T. Cap-specific terminal N 6 -methylation of RNA by an RNA polymerase II-associated methyltransferase. Science, 363:-, 2019 Cited by PubMed Abstract: -methyladenosine (mA), a major modification of messenger RNAs (mRNAs), plays critical roles in RNA metabolism and function. In addition to the internal mA, , 2'--dimethyladenosine (mAm) is present at the transcription start nucleotide of capped mRNAs in vertebrates. However, its biogenesis and functional role remain elusive. Using a reverse genetics approach, we identified PCIF1, a factor that interacts with the serine-5-phosphorylated carboxyl-terminal domain of RNA polymerase II, as a cap-specific adenosine methyltransferase (CAPAM) responsible for -methylation of mAm. The crystal structure of CAPAM in complex with substrates revealed the molecular basis of cap-specific mA formation. A transcriptome-wide analysis revealed that -methylation of mAm promotes the translation of capped mRNAs. Thus, a cap-specific mA writer promotes translation of mRNAs starting from mAm. PubMed: 30467178DOI: 10.1126/science.aav0080 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
