6IW6

Crystal structure of the Lin28-interacting module of human TUT4

Summary for 6IW6

• Entry DOI: 10.2210/pdb6iw6/pdb
• Descriptor: Terminal uridylyltransferase 4,Terminal uridylyltransferase 4, ZINC ION, CITRATE ANION, ... (5 entities in total)
• Functional Keywords: tut4, transferase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 104658.35

Authors

Yamashita, S.,Tomita, K. (deposition date: 2018-12-04, release date: 2019-04-24, Last modification date: 2023-11-22)

Primary citation

Yamashita, S.,Nagaike, T.,Tomita, K.
Crystal structure of the Lin28-interacting module of human terminal uridylyltransferase that regulates let-7 expression.
Nat Commun, 10:1960-1960, 2019

PubMed Abstract: Lin28-dependent oligo-uridylylation of precursor let-7 (pre-let-7) by terminal uridylyltransferase 4/7 (TUT4/7) represses let-7 expression by blocking Dicer processing, and regulates cell differentiation and proliferation. The interaction between the Lin28:pre-let-7 complex and the N-terminal Lin28-interacting module (LIM) of TUT4/7 is required for pre-let-7 oligo-uridylylation by the C-terminal catalytic module (CM) of TUT4/7. Here, we report crystallographic and biochemical analyses of the LIM of human TUT4. The LIM consists of the N-terminal Cys2His2-type zinc finger (ZF) and the non-catalytic nucleotidyltransferase domain (nc-NTD). The ZF of LIM adopts a distinct structural domain, and its structure is homologous to those of double-stranded RNA binding zinc fingers. The interaction between the ZF and pre-let-7 stabilizes the Lin28:pre-let-7:TUT4 ternary complex, and enhances the oligo-uridylylation reaction by the CM. Thus, the ZF in LIM and the zinc-knuckle in the CM, which interacts with the oligo-uridylylated tail, together facilitate Lin28-dependent pre-let-7 oligo-uridylylation.

PubMed: 31036859
DOI: 10.1038/s41467-019-09966-5

Experimental method

X-RAY DIFFRACTION (2.402 Å)