8IDF

Crystal structure of human TUT1 complexed with U6 snRNA

8IDF の概要

• エントリーDOI: 10.2210/pdb8idf/pdb
• 分子名称: Speckle targeted PIP5K1A-regulated poly(A) polymerase, RNA (53-MER), ZINC ION (3 entities in total)
• 機能のキーワード: nucleotidyl transferase, transferase, transferase-rna complex, transferase/rna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75516.79

構造登録者

Yamashita, S.,Tomita, K. (登録日: 2023-02-13, 公開日: 2023-08-09, 最終更新日: 2023-08-23)

主引用文献

Yamashita, S.,Tomita, K.
Mechanism of U6 snRNA oligouridylation by human TUT1.
Nat Commun, 14:4686-4686, 2023

PubMed Abstract: U6 snRNA is a catalytic RNA responsible for pre-mRNA splicing reactions and undergoes various post-transcriptional modifications during its maturation process. The 3'-oligouridylation of U6 snRNA by the terminal uridylyltransferase, TUT1, provides the Lsm-binding site in U6 snRNA for U4/U6 di-snRNP formation and this ensures pre-mRNA splicing. Here, we present the crystal structure of human TUT1 (hTUT1) complexed with U6 snRNA, representing the post-uridylation of U6 snRNA by hTUT1. The N-terminal ZF-RRM and catalytic palm clamp the single-stranded AUA motif between the 5'-short stem and the 3'-telestem of U6 snRNA, and the ZF-RRM specifically recognizes the AUA motif. The ZF and the fingers hold the telestem, and the 3'-end of U6 snRNA is placed in the catalytic pocket of the palm for oligouridylation. The oligouridylation of U6 snRNA depends on the internal four-adenosine tract in the 5'-part of the telestem of U6 snRNA, and hTUT1 adds uridines until the internal adenosine tract can form base-pairs with the 3'-oligouridine tract. Together, the recognition of the specific structure and sequence of U6 snRNA by the multi-domain TUT1 protein and the intrinsic sequence and structure of U6 snRNA ensure the oligouridylation of U6 snRNA.

PubMed: 37563152
DOI: 10.1038/s41467-023-40420-9

実験手法

X-RAY DIFFRACTION (3.7 Å)