1bc5
From Proteopedia
|
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 , and as ligands. Active as Protein-glutamate O-methyltransferase, with EC number 2.1.1.80 Known structural/functional Site: . 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
Page seeded by OCA on Thu Feb 21 11:53:42 2008
