Letter | Published:

Chemotaxis receptor recognition by protein methyltransferase CheR

Nature Structural Biology volume 5, pages 446450 (1998) | Download Citation

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Abstract

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-termini 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.

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Affiliations

  1. Howard Hughes Medical Institute, Center for Advanced Biotechnology and Medicine, and Department of Biochemistry, University of Medicine and Dentistry of New Jersey, 679 Hoes Lane, Piscataway, New Jersey 08854-5638, USA.

    • Snezana Djordjevic
    •  & Ann M. Stock

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Correspondence to Ann M. Stock.

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DOI

https://doi.org/10.1038/nsb0698-446

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