Chemotaxis receptor recognition by protein methyltransferase CheR

S. Djordjevic, Ann Stock

Research output: Contribution to journalArticle

73 Scopus citations


Signal transduction processes commonly involve reversible covalent modifications of receptors. Bacterial chemotaxis receptors are reversibly methylated at specific glutamate residues within coiled-coil regions of their cytoplasmic domains. Methylation is catalyzed by an S-adenosylmethionine- dependent protein methyltransferase, CheR, that binds to a specific sequence at the C-terminal of some chemotaxis receptors. From this tethering point, CheR methylates neighboring receptor molecules. We report the crystal structure, determined to 2.2 Å resolution, of a complex of the Salmonella typhimurium methyltransferase CheR bound to the methylation reaction product, S-adenosylhomocysteine (AdoHcy), and the C-terminal pentapeptide of the aspartate receptor, Tar. The structure indicates the basis for the specificity of interaction between the chemoreceptors and CheR and identifies a specific receptor binding motif incorporated in the CheR methyltransferase domain.

Original languageEnglish (US)
Pages (from-to)446-450
Number of pages5
JournalNature structural biology
Issue number6
StatePublished - Jun 20 1998

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

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