Dear Jacob, We recently solved crystal structures of apo and ligand bound forms of a cofactor S-adenosyl-methionine (SAM) dependent methyltransferase RlmJ (http://nar.oxfordjournals.org/content/41/20/9537.long). Comparison of the structures revealed that binding of the cofactor and a substrate analogue adenosine monophosphate (AMP) to RlmJ induces major structural rearrangements in the four loop regions surrounding the active site. The N-terminal tail undergoes a large movement (88 deg rotation) to cover the cofactor binding site and a neighboring loop region transforms into an α-helix.
Avinash -- Avinash S. Punekar Department of Cell and Molecular Biology Uppsala University
