1bc5
From Proteopedia
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CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER
Overview
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.
About this Structure
1BC5 is a Single protein structure of sequence from Salmonella typhimurium with CO, ACE and SAH as ligands. Active as Protein-glutamate O-methyltransferase, with EC number 2.1.1.80 Structure known Active Site: COB. Full crystallographic information is available from OCA.
Reference
Chemotaxis receptor recognition by protein methyltransferase CheR., Djordjevic S, Stock AM, Nat Struct Biol. 1998 Jun;5(6):446-50. PMID:9628482
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