7C38
Crystal structure of AofleA from Arthrobotrys oligospora in complex with L-fucose
Summary for 7C38
Entry DOI | 10.2210/pdb7c38/pdb |
Related | 7C37 |
Descriptor | AofleA, alpha-L-fucopyranose, beta-L-fucopyranose, ... (5 entities in total) |
Functional Keywords | nematode-trapping fungi, arthrobotrys oligospora, fucose-specific lectin, sugar binding protein |
Biological source | Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491) (Nematode-trapping fungus) |
Total number of polymer chains | 2 |
Total formula weight | 80626.11 |
Authors | |
Primary citation | Liu, M.,Cheng, X.,Wang, J.,Tian, D.,Tang, K.,Xu, T.,Zhang, M.,Wang, Y.,Wang, M. Structural insights into the fungi-nematodes interaction mediated by fucose-specific lectin AofleA from Arthrobotrys oligospora. Int.J.Biol.Macromol., 164:783-793, 2020 Cited by PubMed Abstract: Fungal lectin can bind specific carbohydrate structures of the host and work in recognition and adhesion or as a toxic factor. AofleA, as a fucose-specific lectin from widely studied nematode predatory fungus Arthrobotrys oligospora, possibly plays a key role in the event of capturing nematodes, but the mechanism remains unknown. Here we report the crystal structure of AofleA, which exists as a homodimer with each subunit folds as a six-bladed β-propeller. Our structural and biological results revealed that three of the six putative binding sites of AofleA had fucose-binding abilities. In addition, we found that AofleA could bind to the pharynx and intestine of the nematode in a fucose-binding-dependent manner. Our results facilitate the understanding of the mechanism that fucose-specific lectin mediates fungi-nematodes interaction, and provide structural information for the development of potential applications of AofleA. PubMed: 32698064DOI: 10.1016/j.ijbiomac.2020.07.173 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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