The ETR1 receptor from Arabidopsis binds the gaseous hormone ethylene, A co
pper ion associated with the ethylene-binding domain is required for high-a
ffinity ethylene-binding activity. A missense mutation in the domain that r
enders the plant insensitive to ethylene eliminates both ethylene binding a
nd the interaction of topper with the receptor. A sequence from the genome
of the cyanobacterium Synechocystis sp, strain 6803 that shows homology to
the ethylene-binding domain of ETR1 encodes a functional ethylene-binding p
rotein. On the basis of sequence conservation between the Arabidopsis and t
he cyanobacterial ethylene-binding domains and on in vitro mutagenesis of E
TR1, a structural model for this copper-based ethylene sensor domain is pre
sented.