The LuxCDE complex is involved in bioluminescence (emission of light by an
organism), recycling and recruiting fatty acids into the long-chain aldehyde
substrate required for the luminescent reaction. The subunits( a
transferase, a synthetase, and a reductase) assemble to form a 500 kDa fatty
acid reductase complex. Each subunit generates a fatty-acid
intermediate which is passed to another subunit by a channeling mechanism.
Our lab is interested in this channeling mechanism, and for this purpose
we are pursuing a structural study of the LuxCDE complex.
The recombinant C subunit, the acyl-CoA reductase (58 kDa) has been
crystallized and multiple anomalous diffraction (MAD) data collected to 2.9A
resolution. We are currently in the process of solving the structure of
this subunit, which, in addition to insights into this part of the
bioluminescence mechanism, will make it easier to solve the structure of the