11JF

RNA Vault bound to PARP4 MINT, focused refinement (MVP/PARP4/TEP1 NADP sample)

Summary for 11JF

• Entry DOI: 10.2210/pdb11jf/pdb
• EMDB information: 75735
• Descriptor: Major vault protein, Protein mono-ADP-ribosyltransferase PARP4 (3 entities in total)
• Functional Keywords: rna vault, complex, tep1, parp4, structural protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 391715.70

Authors

Osinski, A.,Tagliabracci, V.S. (deposition date: 2026-02-26, 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

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: 42146377
DOI: 10.64898/2026.05.01.722283

Experimental method

ELECTRON MICROSCOPY (2.85 Å)