MG517 is an essential glycosyl-transferase of the pathogenic organism Mycoplasma genitalium that regulates the membrane fluidity . The N-terminal region of this protein was modeled by means of homology modeling and Molecular Dynamics  but the structure of its C-terminal extension remains elusive. MG517 needs to be attached to the membrane in order to be active and it has been suggested that the C-terminus has an important role in this adhesion . We report here a computational strategy to study this region and to find structural elements of MG517 possibly associated to membranes . The combination of predictor servers and modeling has allowed us to identify a 23 residues long amphipathic helix in the apical extreme of the C-terminal extension. The membrane association process of this helix has been simulated by Molecular Dynamics and Metadynamics. We have experimentally verified that truncation of part of this helix causes a substantial reduction of glycoglycerolipids synthesis. The model proposes that MG517 recognizes and binds the diacylglycerol substrate embedded in the membrane by means of this α-helix at the C-terminus together with a previously identified binding pocket at the N-terminus .
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