11GZ
TEP1 TIR/DUF4062 domain
Summary for 11GZ
| Entry DOI | 10.2210/pdb11gz/pdb |
| Descriptor | Telomerase protein component 1, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | nad-ase, tir domain, duf4062, tep1, rna vault, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 25626.98 |
| Authors | Osinski, A.,Tomchick, D.R.,Tagliabracci, V.S. (deposition date: 2026-02-23, release date: 2026-05-20, Last modification date: 2026-06-03) |
| Primary citation | Osinski, A.,Mayro, B.,Lopez, V.A.,Schrad, J.,Choi, H.,Tomchick, D.R.,Pawlowski, K.,Forsberg, K.,Shahmoradian, S.H.,Tagliabracci, V.S. TIR-like NADases act in bacterial immunity and the RNA vault. Biorxiv, 2026 Cited by PubMed Abstract: Across all domains of life, organisms exploit NAD metabolism as a central line of defense against invading pathogens. Here, we show that domain of unknown function 4062 (DUF4062) is a widespread family of TIR-like NADases that hydrolyze NAD to ADP-ribose and nicotinamide. In bacteria, DUF4062 homologs form a previously unrecognized antiphage defense system, which we name Swarożyc, that assembles with the phage portal into a supramolecular NADase complex to induce abortive infection. In eukaryotes, DUF4062 is found in TEP1, which we demonstrate functions as an active NADase within the RNA vault, an enigmatic organelle-like structure. Single-particle cryo-electron microscopy reveals ADP-ribose bound within the shoulder of both reconstituted and human brain vaults, while cryo-electron tomography positions TEP1 along the central axis at the shoulder. Thus, TEP1, like bacterial Swarożyc, functions by depleting NAD , providing new insight into the long-standing mystery of vault function. PubMed: 42146377DOI: 10.64898/2026.05.01.722283 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.44 Å) |
Structure validation
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