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11EE

RNA Vault shoulder region with BAD bound, focused refinement (MVP/TEP1 sample)

Summary for 11EE
Entry DOI10.2210/pdb11ee/pdb
EMDB information75647
DescriptorMajor vault protein, [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl [(2R,3S,4R,5S)-5-(3-carbamoylphenyl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate (non-preferred name) (3 entities in total)
Functional Keywordsrna vault, adpr, adp-ribose, major vault protein, structural protein
Biological sourceHomo sapiens (human)
Total number of polymer chains3
Total formula weight300345.61
Authors
Osinski, A.,Tagliabracci, V.S. (deposition date: 2026-02-18, release date: 2026-05-20, Last modification date: 2026-06-03)
Primary citationOsinski, 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: 42146377
DOI: 10.64898/2026.05.01.722283
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (1.87 Å)
Structure validation

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PDB entries from 2026-07-01

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