Abstract
CheA is a multi-domain histidine kinase which has been demonstrated to play a role in the chemosensory array in Escherichia coli, Salmonella typhimurium, Thermotoga maritima and related enterobacteria. The P4 domain of CheA is of particular interest due to its role in catalyzing ATP/ADP conversion, a process which involves Mg2+ in the ATP-binding pocket of the enzyme. Recent studies in GHKL superfamily members MutL (from E coli) and BCK (from Rattus norvegicus) demonstrate improved activity in the presence of monovalent cations Na+ and K+. Here we present results from a combined experimental and computational analysis to assess the effect of monovalent cations on the activity of Salmonella typhimurium CheA and subsequent phosphor-transfer to response regulator CheY.
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