5WU3

Crystal structure of human Tut1 bound with MgUTP, form II

Summary for 5WU3

• Entry DOI: 10.2210/pdb5wu3/pdb
• Related: 5WU1 5WU2 5WU4 5WU5 5WU6
• Descriptor: Speckle targeted PIP5K1A-regulated poly(A) polymerase, URIDINE 5'-TRIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: terminal nucleotidyl transferase, transferase
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus, nucleolus : Q9H6E5
• Total number of polymer chains: 2
• Total formula weight: 125719.11

Authors

Yamashita, S.,Tomita, K. (deposition date: 2016-12-16, release date: 2017-05-31, Last modification date: 2023-11-08)

Primary citation

Yamashita, S.,Takagi, Y.,Nagaike, T.,Tomita, K.
Crystal structures of U6 snRNA-specific terminal uridylyltransferase
Nat Commun, 8:15788-15788, 2017

PubMed Abstract: The terminal uridylyltransferase, TUT1, builds or repairs the 3'-oligo-uridylylated tail of U6 snRNA. The 3'-oligo-uridylylated tail is the Lsm-binding site for U4/U6 di-snRNP formation and U6 snRNA recycling for pre-mRNA splicing. Here, we report crystallographic and biochemical analyses of human TUT1, which revealed the mechanisms for the specific uridylylation of the 3'-end of U6 snRNA by TUT1. The O and O atoms of the UTP base form hydrogen bonds with the conserved His and Asn in the catalytic pocket, respectively, and TUT1 preferentially incorporates UMP onto the 3'-end of RNAs. TUT1 recognizes the entire U6 snRNA molecule by its catalytic domains, N-terminal RNA-recognition motifs and a previously unidentified C-terminal RNA-binding domain. Each domain recognizes specific regions within U6 snRNA, and the recognition is coupled with the domain movements and U6 snRNA structural changes. Hence, TUT1 functions as the U6 snRNA-specific terminal uridylyltransferase required for pre-mRNA splicing.

PubMed: 28589955
DOI: 10.1038/ncomms15788

Experimental method

X-RAY DIFFRACTION (2.703 Å)