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Open data
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Basic information
| Entry | Database: PDB / ID: 21zt | |||||||||||||||||||||
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| Title | Cryo-EM structure of TLP-2 | |||||||||||||||||||||
Components | TLP-2 | |||||||||||||||||||||
Keywords | CARBOHYDRATE / Glycofibril | |||||||||||||||||||||
| Biological species | algae metagenome (others) | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||||||||||||||
Authors | Yan, N. / Li, Z. / Wang, T. | |||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Cell Chem Biol / Year: 2026Title: CryoSeek identification of glycofibrils with diverse compositions and structural assemblies. Authors: Zhangqiang Li / Tongtong Wang / Yitong Sun / Kui Xu / Wenze Huang / Qiangfeng Cliff Zhang / Chuangye Yan / Mingxu Hu / Nieng Yan / ![]() Abstract: CryoSeek is a research strategy that employs cryo-electron microscopy (cryo-EM) to discover bio-entities from accessible sources, supplemented with AI-facilitated data processing and bioinformatic ...CryoSeek is a research strategy that employs cryo-electron microscopy (cryo-EM) to discover bio-entities from accessible sources, supplemented with AI-facilitated data processing and bioinformatic analyses. Here we report CryoSeek-based characterization of more glycofibrils isolated from the Tsinghua Lotus Pond (TLP), named TLP-0/2/3/4b/IPT, with resolutions ranging from 3.0-3.5 Å. These glycofibrils, all covered with dense glycoshells, have various mass percentiles of the central protein components. TLP-0 has no protein at all, TLP-2 and TLP-4b each only have a linear chain of di- or tetra-peptide repeats, respectively; the central stem of TLP-3 is a trimer of linear tripeptide repeats, and IPT (immunoglobulin-like, plexins, and transcription factors) refers to the tandem domain that constitutes the central stem of TLP-IPT. Glycan-mediated interactions determine the structural assembly of the glycofibrils that lack folded protein component. Our previous and current studies reveal the diversity of the structural folds of glycans, advance our understanding of glycan architecture, and further demonstrate CryoSeek as a structure-first paradigm for discovery. | |||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 21zt.cif.gz | 40.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb21zt.ent.gz | 38.9 KB | Display | PDB format |
| PDBx/mmJSON format | 21zt.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1z/21zt ftp://data.pdbj.org/pub/pdb/validation_reports/1z/21zt | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 68122MC ![]() 21nrC ![]() 21nsC ![]() 21ntC ![]() 22agC M: map data used to model this data C: citing same article ( |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein/peptide | Mass: 650.638 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) algae metagenome (others) | ||||
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| #2: Polysaccharide | alpha-L-arabinofuranose-(1-4)-alpha-D-mannopyranose-(1-2)-alpha-L-arabinofuranose-(1-2)-beta-L- ...alpha-L-arabinofuranose-(1-4)-alpha-D-mannopyranose-(1-2)-alpha-L-arabinofuranose-(1-2)-beta-L-arabinofuranose-(1-2)-alpha-L-arabinofuranose-(1-2)-[alpha-L-arabinofuranose-(1-2)-beta-D-xylopyranose-(1-3)-beta-D-glucopyranose-(1-3)][alpha-L-arabinofuranose-(1-6)]alpha-D-mannopyranose-(1-2)-alpha-L-arabinofuranose-(1-2)-beta-L-arabinofuranose-(1-3)-[beta-D-xylopyranose-(1-3)-beta-D-xylopyranose-(1-3)-beta-D-xylopyranose-(1-4)-[alpha-L-arabinofuranose-(1-2)]beta-D-xylopyranose-(1-4)][alpha-L-arabinofuranose-(1-2)-alpha-L-arabinofuranose-(1-2)]beta-D-xylopyranose-(1-4)-[alpha-L-arabinofuranose-(1-2)-[alpha-L-arabinofuranose-(1-4)]beta-D-xylopyranose-(1-2)-[alpha-L-arabinofuranose-(1-3)]alpha-D-glucopyranose-(1-5)-alpha-L-arabinofuranose-(1-5)-alpha-L-arabinofuranose-(1-2)-[beta-D-glucopyranose-(1-3)]alpha-L-arabinofuranose-(1-4)-[beta-L-arabinofuranose-(1-2)-alpha-L-arabinofuranose-(1-2)-[beta-D-xylopyranose-(1-3)]beta-L-arabinofuranose-(1-2)][alpha-L-arabinofuranose-(1-3)-beta-D-xylopyranose-(1-3)]beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-3)]2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose Type: oligosaccharide / Mass: 5339.562 Da / Num. of mol.: 4 / Source method: obtained synthetically Has ligand of interest | N | Has protein modification | N | |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
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Sample preparation
| Component | Name: TLP-2 / Type: COMPLEX / Entity ID: #1 / Source: NATURAL |
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| Source (natural) | Organism: algae metagenome (others) |
| Buffer solution | pH: 7 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: DIFFRACTION / Nominal defocus max: 1800 nm / Nominal defocus min: 1300 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
| Helical symmerty | Angular rotation/subunit: 108.7 ° / Axial rise/subunit: 6.2 Å / Axial symmetry: C1 | |||||||||
| 3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 16082 / Symmetry type: HELICAL |
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