7C37

Crystal structure of AofleA from Arthrobotrys oligospora

Summary for 7C37

• Entry DOI: 10.2210/pdb7c37/pdb
• Descriptor: AofleA, BICINE (3 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: 79597.17

Authors

Liu, M.,Cheng, X.,Wang, J.,Zhang, M.,Wang, M. (deposition date: 2020-05-11, release date: 2020-07-29, Last modification date: 2023-11-29)

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

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: 32698064
DOI: 10.1016/j.ijbiomac.2020.07.173

Experimental method

X-RAY DIFFRACTION (1.451 Å)