The Helicobacter pylori GatCAB which plays a vital role in maintaining translational fidelity, catalyzes three reactions: (i) hydrolysis of Glutamine at the active site of its GatA subunit; (ii) phosphorylation of misacylated Glu-tRNAGln; and (iii) transamidation of phosphorylated Glu-tRNAGln to Gln-tRNAGln at the GatB active site. Ammonia required for transamidation at the GatB active site is assumed to come from NH3 released at the GatA active site, through an intra -molecular tunnel that connects both active sites. This ammonia transfer suggests a form of coupling between the GatA and GatB subunits. Molecular dynamics simulations have been carried out on wild type and three mutant GatCAB models. The trajectories have been used to study the changes in correlation patterns and RMSD variations of mutants with respect to the wild-type. These changes suggest the existence of a bidirectional communication pathway between GatA and GatB subunits.

Computational study of the possible coupling between subunits of the enzyme glutamine-dependent amidotransferase (GatCAB)

244th National Meeting (2012)

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