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 Cited by 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: 9628482DOI: 10.1038/nsb0698-446 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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