5W0B

Structure of human TUT7 catalytic module (CM)

5W0B の概要

• エントリーDOI: 10.2210/pdb5w0b/pdb
• 分子名称: Terminal uridylyltransferase 7, ZINC ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: terminal uridyltransferase, tutase, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 135284.00

構造登録者

Faehnle, C.R.,Walleshauser, J.,Joshua-Tor, L. (登録日: 2017-05-30, 公開日: 2017-06-28, 最終更新日: 2024-03-13)

主引用文献

Faehnle, C.R.,Walleshauser, J.,Joshua-Tor, L.
Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis.
Nat. Struct. Mol. Biol., 24:658-665, 2017

PubMed Abstract: The uridyl transferases TUT4 and TUT7 (collectively called TUT4(7)) switch between two modes of activity, either promoting expression of let-7 microRNA (monoU) or marking it for degradation (oligoU). Lin28 modulates the switch via recruitment of TUT4(7) to the precursor pre-let-7 in stem cells and human cancers. We found that TUT4(7) utilize two multidomain functional modules during the switch from monoU to oligoU. The catalytic module (CM) is essential for both activities, while the Lin28-interacting module (LIM) is indispensable for oligoU. A TUT7 CM structure trapped in the monoU activity staterevealed a duplex-RNA-binding pocket that orients group II pre-let-7 hairpins to favor monoU addition. Conversely, the switch to oligoU requires the ZK domain of Lin28 to drive the formation of a stable ternary complex between pre-let-7 and the inactive LIM. Finally, ZK2 of TUT4(7) aids oligoU addition by engaging the growing oligoU tail through uracil-specific interactions.

PubMed: 28671666
DOI: 10.1038/nsmb.3428

実験手法

X-RAY DIFFRACTION (2.614 Å)