This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bc5
From Proteopedia
| Line 4: | Line 4: | ||
==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== | ||
| Line 15: | Line 15: | ||
[[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]] | ||
| Line 24: | Line 24: | ||
[[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
|
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
