8IDF
Crystal structure of human TUT1 complexed with U6 snRNA
Summary for 8IDF
| Entry DOI | 10.2210/pdb8idf/pdb |
| Descriptor | Speckle targeted PIP5K1A-regulated poly(A) polymerase, RNA (53-MER), ZINC ION (3 entities in total) |
| Functional Keywords | nucleotidyl transferase, transferase, transferase-rna complex, transferase/rna |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 75516.79 |
| Authors | Yamashita, S.,Tomita, K. (deposition date: 2023-02-13, release date: 2023-08-09, Last modification date: 2023-08-23) |
| Primary citation | Yamashita, S.,Tomita, K. Mechanism of U6 snRNA oligouridylation by human TUT1. Nat Commun, 14:4686-4686, 2023 Cited by 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: 37563152DOI: 10.1038/s41467-023-40420-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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