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 entire complex.