5FSC
Structure of tectonin 2 from Laccaria bicolor in complex with allyl- alpha_4-methyl-mannoside
Summary for 5FSC
Entry DOI | 10.2210/pdb5fsc/pdb |
Related | 5FSB |
Descriptor | TECTONIN 2, MAGNESIUM ION, prop-2-en-1-yl 4-O-methyl-alpha-D-mannopyranoside, ... (4 entities in total) |
Functional Keywords | sugar binding protein, lectin, methylated sugar, nematoxic, beta-propeller |
Biological source | LACCARIA BICOLOR |
Total number of polymer chains | 2 |
Total formula weight | 49783.28 |
Authors | Sommer, R.,Bleuer, S.,Titz, A.,Kunzler, M.,Varrot, A. (deposition date: 2016-01-04, release date: 2017-03-29, Last modification date: 2024-01-10) |
Primary citation | Sommer, R.,Makshakova, O.N.,Wohlschlager, T.,Hutin, S.,Marsh, M.,Titz, A.,Kunzler, M.,Varrot, A. Crystal Structures of Fungal Tectonin in Complex with O-Methylated Glycans Suggest Key Role in Innate Immune Defense. Structure, 26:391-402.e4, 2018 Cited by PubMed Abstract: Innate immunity is the first line of defense against pathogens and predators. To initiate a response, it relies on the detection of invaders, where lectin-carbohydrate interactions play a major role. O-Methylated glycans were previously identified as non-self epitopes and conserved targets for defense effector proteins belonging to the tectonin superfamily. Here, we present two crystal structures of Tectonin 2 from the mushroom Laccaria bicolor in complex with methylated ligands, unraveling the molecular basis for this original specificity. Furthermore, they revealed the formation of a ball-shaped tetramer with 24 binding sites distributed at its surface, resembling a small virus capsid. Based on the crystal structures, a methylation recognition motif was identified and found in the sequence of many tectonins from bacteria to human. Our results support a key role of tectonins in innate defense based on a distinctive and conserved type of lectin-glycan interaction. PubMed: 29398527DOI: 10.1016/j.str.2018.01.003 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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