1BC5

CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER

Summary for 1BC5

• Entry DOI: 10.2210/pdb1bc5/pdb
• Descriptor: CHEMOTAXIS RECEPTOR METHYLTRANSFERASE, CHEMOTAXIS RECEPTOR, COBALT (II) ION, ... (5 entities in total)
• Functional Keywords: methyltransferase, peptide binding, chemotaxis receptor, complex (methyltransferase-peptide), complex (methyltransferase-peptide) complex, complex (methyltransferase/peptide)
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 2
• Total formula weight: 32157.49

Authors

Djordjevic, S.,Stock, A.M. (deposition date: 1998-05-05, release date: 1998-11-25, Last modification date: 2024-11-06)

Primary citation

Djordjevic, S.,Stock, A.M.
Chemotaxis receptor recognition by protein methyltransferase CheR.
Nat.Struct.Biol., 5:446-450, 1998

PubMed 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 A 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.

PubMed: 9628482
DOI: 10.1038/nsb0698-446

Experimental method

X-RAY DIFFRACTION (2.2 Å)