9UFE
Cryo-EM structure of the tubular mastigoneme (the central tube) from golden algae 2.17 angstrom resolution
This is a non-PDB format compatible entry.
Summary for 9UFE
| Entry DOI | 10.2210/pdb9ufe/pdb |
| EMDB information | 64106 |
| Descriptor | OCM5, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-xylopyranose-(1-2)-beta-D-xylopyranose-(1-6)-[beta-D-xylopyranose-(1-3)][2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-[beta-D-xylopyranose-(1-3)]alpha-D-mannopyranose-(1-6)][beta-D-xylopyranose-(1-2)]alpha-D-mannopyranose-(1-6)-[beta-D-mannopyranose-(1-2)][alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (25 entities in total) |
| Functional Keywords | cryo-em, tubular mastigoneme, golden algae, n-glycans, carbohydrate |
| Biological source | Ochromonas danica More |
| Total number of polymer chains | 18 |
| Total formula weight | 1006780.47 |
| Authors | |
| Primary citation | Huang, J.,Tao, H.,Chen, S.,Cui, Y.,Xu, Y.,Yan, C.,Yan, N. Structural N- and O-glycans revealed by high-resolution cryo-EM analysis of tubular mastigonemes. Science, :eaef4958-eaef4958, 2026 Cited by PubMed Abstract: The chemical complexity and non-templated biosynthesis of glycans have posed significant challenges for establishing sequence-structure relationships. Here we report cryo-EM structures of tubular mastigonemes from a golden alga species, , in which a large number of N- and O-glycans are resolved at 1.8-2.2 Å resolution. Beyond high-mannose and complex N-glycans, we identify a non-canonical N-glycan on the Ala--Asp (AD) motif. The surface spikes comprise dense O-glycans coating PSXX tetrapeptide repeats, with two glycans linked on trihydroxylated proline and one on serine per repeat. In addition to various types of sugars and their covalent modifiers, water molecules (>10% of resolved volume) and cations are clearly resolved and mediate the structural assembly. Our study establishes a framework for investigating glycan folding in high-order biological assemblies. PubMed: 42024774DOI: 10.1126/science.aef4958 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.17 Å) |
Structure validation
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