5THM

Esterase-6 from Drosophila melanogaster

Summary for 5THM

• Entry DOI: 10.2210/pdb5thm/pdb
• Descriptor: Esterase-6, N,N-dimethylboranamine (3 entities in total)
• Functional Keywords: carboxylesterase, hydrolase
• Biological source: Drosophila melanogaster (Fruit fly)
• Cellular location: Secreted: P08171
• Total number of polymer chains: 1
• Total formula weight: 60970.68

Authors

Fraser, N.J.,Jackson, C.J. (deposition date: 2016-09-29, release date: 2017-03-08, Last modification date: 2023-10-04)

Primary citation

Younus, F.,Fraser, N.J.,Coppin, C.W.,Liu, J.W.,Correy, G.J.,Chertemps, T.,Pandey, G.,Maibeche, M.,Jackson, C.J.,Oakeshott, J.G.
Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila.
Sci Rep, 7:46188-46188, 2017

PubMed Abstract: Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.

PubMed: 28393888
DOI: 10.1038/srep46188

Experimental method

X-RAY DIFFRACTION (2.15 Å)