Active site of the enzyme which demethylates receptors during bacterial chemotaxis

S. A. Simms, E. W. Cornman, J. Mottonen, J. Stock

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

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 β-α-β motif found in a number of nucleotide binding proteins associated with receptor function in vertebrate tissues. A central feature of this sturcture 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.

Original languageEnglish (US)
Pages (from-to)29-31
Number of pages3
JournalJournal of Biological Chemistry
Volume262
Issue number1
StatePublished - Jan 1 1987

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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