6LQK
Crystal structure of honeybee RyR NTD
Summary for 6LQK
Entry DOI | 10.2210/pdb6lqk/pdb |
Descriptor | ryanodine receptor, MAGNESIUM ION (3 entities in total) |
Functional Keywords | honey bee, ryanodine receptor, n-terminal domain, crystal structure., membrane protein |
Biological source | Apis mellifera (Honeybee) |
Total number of polymer chains | 2 |
Total formula weight | 44395.63 |
Authors | |
Primary citation | Zhou, Y.,Wang, W.,Salauddin, N.M.,Lin, L.,You, M.,You, S.,Yuchi, Z. Crystal structure of the N-terminal domain of ryanodine receptor from the honeybee, Apis mellifera. Insect Biochem.Mol.Biol., 125:103454-103454, 2020 Cited by PubMed Abstract: Ryanodine receptors (RyRs) are the molecular target of diamides, a new chemical class of insecticides. Diamide insecticides are used to control lepidopteran pests and were considered relatively safe for mammals and non-targeted beneficial insects, including honey bees. However, recent studies showed that exposure to diamides could cause long-lasting locomotor deficits of bees. Here we report the crystal structure of RyR N-terminal domain A (NTD-A) from the honeybee, Apis mellifera, at 2.5 Å resolution. It shows a similar overall fold as the RyR NTD-A from mammals and the diamondback moth (DBM), Plutella xylostella, and still several loops located at the inter-domain interfaces show insect-specific or bee-specific structural features. A potential insecticide-binding pocket formed by loop9 and loop13 is conserved in lepidopteran but different in both mammals and bees, making it a good candidate targeting site for the development of pest-selective insecticides. Furthermore, a conserved intra-domain disulfide bond was observed in both DBM and bee RyR NTD-A crystal structures, which explains their higher thermal stability compared to mammalian RyR NTD-A. This work provides a basis for the development of novel insecticides with better selectivity between pests and bees by targeting a distinct site on pest RyRs, which would be a promising strategy to overcome the current toxicity problem. PubMed: 32781205DOI: 10.1016/j.ibmb.2020.103454 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.499 Å) |
Structure validation
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