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J. Biol. Chem., Vol. 262, Issue 1, 29-31, 01, 1987

Active site of the enzyme which demethylates receptors during bacterial chemotaxis

SA Simms, EW Cornman, J Mottonen and J Stock

The CheB methylesterase catalyzes the hydrolysis of glutamyl methyl esters in bacterial chemoreceptor proteins. Studies with residue- specific inhibitors suggest that a cysteine residue is required. The nucleotide sequence of the cheB gene predicts a 349-amino acid protein with cysteine residues at positions 207 and 309. Oligonucleotide- directed mutagenesis was used to change each cysteine to an alanine. Whereas the Cys207-Ala mutation had essentially no effect on esterase activity, the Cys309-Ala mutation caused a complete inactivation of the enzyme. Cys309 is located adjacent to a sequence of amino acids which is characteristic of the beta-alpha-beta motif found in a number of nucleotide binding proteins associated with receptor function in vertebrate tissues. A central feature of this structure is Gly-X-Gly-X- X-Gly. Mutation of the second glycine in this region (Gly284) to a valine also caused a complete loss of esterase activity.
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