1bc5
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 1BC5 is a | + | 1BC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with CO, ACE and SAH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-glutamate_O-methyltransferase Protein-glutamate O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.80 2.1.1.80] Structure known Active Site: COB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BC5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peptide binding]] | [[Category: peptide binding]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:54:05 2007'' |
Revision as of 11:48, 5 November 2007
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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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