1bc5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Signal transduction processes commonly involve reversible covalent | + | 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Djordjevic, S.]] | [[Category: Djordjevic, S.]] | ||
| - | [[Category: Stock, A | + | [[Category: Stock, A M.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CO]] | [[Category: CO]] | ||
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[[Category: peptide binding]] | [[Category: peptide binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:42 2008'' |
Revision as of 09:53, 21 February 2008
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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 , 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
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