6IRV

Crystal structure of the human cap-specific adenosine methyltransferase

6IRV の概要

• エントリーDOI: 10.2210/pdb6irv/pdb
• 分子名称: Phosphorylated CTD-interacting factor 1 (2 entities in total)
• 機能のキーワード: rna methylation, methyltransferase, m6a, n6-methyladenosine, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 118786.05

構造登録者

Hirano, S.,Nishimasu, H.,Ishitani, R.,Nureki, O. (登録日: 2018-11-14, 公開日: 2018-12-05, 最終更新日: 2023-11-22)

主引用文献

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

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: 30467178
DOI: 10.1126/science.aav0080

実験手法

X-RAY DIFFRACTION (2.7 Å)