6N67
Crystal structure of the ligase domain of fungal tRNA ligase Trl1
Summary for 6N67
| Entry DOI | 10.2210/pdb6n67/pdb |
| Descriptor | tRNA ligase, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | rna ligase, trna splicing, inhibitor, atp-binding, ligase |
| Biological source | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) |
| Total number of polymer chains | 1 |
| Total formula weight | 50233.53 |
| Authors | Peschek, J.,Walter, P. (deposition date: 2018-11-26, release date: 2019-07-03, Last modification date: 2024-10-23) |
| Primary citation | Peschek, J.,Walter, P. tRNA ligase structure reveals kinetic competition between non-conventional mRNA splicing and mRNA decay. Elife, 8:-, 2019 Cited by PubMed Abstract: Yeast tRNA ligase (Trl1) is an essential trifunctional enzyme that catalyzes exon-exon ligation during tRNA biogenesis and the non-conventional splicing of mRNA during the unfolded protein response (UPR). The UPR regulates the protein folding capacity of the endoplasmic reticulum (ER). ER stress activates Ire1, an ER-resident kinase/RNase, which excises an intron from mRNA followed by exon-exon ligation by Trl1. The spliced product encodes for a potent transcription factor that drives the UPR. Here we report the crystal structure of Trl1 RNA ligase domain from at 1.9 Å resolution. Structure-based mutational analyses uncovered kinetic competition between RNA ligation and degradation during mRNA splicing. Incompletely processed mRNA is degraded by Xrn1 and the Ski/exosome complex. We establish cleaved mRNA as endogenous substrate for ribosome-associated quality control. We conclude that mRNA decay and surveillance mechanisms collaborate in achieving fidelity of non-conventional mRNA splicing during the UPR. PubMed: 31237564DOI: 10.7554/eLife.44199 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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