ArticleProceedings of the National Academy of Sciences of the United States of America2024
CryoSeek: A strategy for bioentity discovery using cryoelectron microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Cryo-EM: the revolution continues.IUCrJ · 2026Review
- AI-Physics-Experiment Trinity for Integrated Protein Dynamics Modeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Structure of the mouse cytoplasmic lattice.Nature · 2026Article
- Absolute hand determination of glycofibrils from natural sources in cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structure first - exploration and discovery with cryo-electron microscopy.Journal of cell science · 2026Review
- Donor strand complementation and calcium ion coordination drive the chaperone-free polymerization of archaeal cannulae.Nature communications · 2025Article
- Validation of helical symmetry parameters in the EMDB.Acta crystallographica. Section D, Structural biology · 2025Article
- CryoSeek II: Cryo-EM analysis of glycofibrils from freshwater reveals well-structured glycans coating linear tetrapeptide repeats.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Tumor-associated Tn and STn antigens: from molecular mechanism to precision diagnosis and treatment.Frontiers in immunology · 2025Review
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Authors and funding
7 authors.
Funding
Abstract
Structural biology is experiencing a paradigm shift from targeted structural determination to structure-guided discovery of previously uncharacterized bioentities. We employed cryoelectron microscopy (cryo-EM) to analyze filtered water samples collected from the Tsinghua Lotus Pond. Here, we report the structural determination and characterization of two highly similar helical fibrils, named TLP-1a and TLP-1b, each approximately 8 nm in diameter with a 15-Å wide tunnel. These fibrils are assembled from a similar protein protomer, whose structure was conveniently automodeled in CryoNet. The protomer structure does not match any available experimental structures, but shares the same fold as many predicted structures of unknown functions. The amino-terminal β strand of protomer n + 4 inserts into a cleft in protomer n to complete an immunoglobulin (Ig)-like domain. This packing mechanism, known as donor-strand exchange (DSE), has been observed in several bacterial pilus assemblies, wherein the donor is protomer n + 1. Despite distinct shape and thickness, this reminiscence suggests that TLP-1a/b fibrils may represent uncharacterized bacterial pili. Our study demonstrates an emerging paradigm in structural biology, where high-resolution structural determination precedes and drives the identification and characterization of completely unknown objects.
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Registered trials
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