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6LQK

Crystal structure of honeybee RyR NTD

Summary for 6LQK
Entry DOI10.2210/pdb6lqk/pdb
Descriptorryanodine receptor, MAGNESIUM ION (3 entities in total)
Functional Keywordshoney bee, ryanodine receptor, n-terminal domain, crystal structure., membrane protein
Biological sourceApis mellifera (Honeybee)
Total number of polymer chains2
Total formula weight44395.63
Authors
Zhou, Y.,Lin, L.,Yuchi, Z. (deposition date: 2020-01-13, release date: 2021-01-20, Last modification date: 2024-10-23)
Primary citationZhou, 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: 32781205
DOI: 10.1016/j.ibmb.2020.103454
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.499 Å)
Structure validation

226707

数据于2024-10-30公开中

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