Today, our lab published a full article in Nature describing the crystal structure of a 240 kDa core complex of the E. coli C-P lyase, an enzyme required for utilisation of phosphonate compounds in bacteria. Phosphonate are characterised by a direct carbon-phosphorus (C-P) bond, which is stable to hydrolysis and therefore requires a totally different enzymatic machinery. In C-P lyase, cleavage of the bond is achieved using radical chemistry in the subunit PhnJ, which is one of four proteins in the hetero-octameric core complex. We also show, using negative stain electron microscopy, that a fifth subunit, PhnK, an ABC cassette protein, binds as a monomer to the core complex via a conserved loop in PhnJ and breaks the two-fold symmetry of the core.
For more information, have a look at the paper in Nature.
Seweryn, P., Van, L. B., Kjeldgaard, M., Russo, C. J., Passmore, L. A., Hove-Jensen, B., Jochimsen, B., Brodersen, D. E. (2015) “Structural insights into the bacterial carbon-phosphorus lyase machinery”, Nature, 525(7567): 68-72.