1chd | pdb_00001chd

CHEB METHYLESTERASE DOMAIN

spinqualitylabelsall models 1chd, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1chd is a 1 chain structure with sequence from Salty. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: CHEB (SALTY) Activity: Protein-glutamate methylesterase, with EC number 3.1.1.61 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [CHEB_SALTY] Responsible for removing the methyl group from the gamma-glutamyl methyl ester residues in the methyl-accepting chemotaxis proteins (MCP). The MCP methylation state of the cell is crucial for sensory responses and adaptations.[HAMAP-Rule:MF_00099] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Signaling activity of bacterial chemotaxis transmembrane receptors is modulated by reversible covalent modification of specific receptor glutamate residues. The level of receptor methylation results from the activities of a specific S-adenosylmethionine-dependent methyltransferase, CheR, and the CheB methylesterase, which catalyzes hydrolysis of receptor glutamine or methylglutamate side-chains to glutamic acid. The CheB methylesterase belongs to a large family of response regulator proteins in which N-terminal regulatory domains control the activities of C-terminal effector domains. The crystal structure of the catalytic domain of the Salmonella typhimurium CheB methylesterase has been determined at 1.75 A resolution. The domain has a modified, doubly wound alpha/beta fold in which one of the helices is replaced by an anti-parallel beta-hairpin. Previous biochemical and mutagenesis data, suggest that the methylester hydrolysis catalyzed by CheB proceeds through a mechanism involving a serine nucleophile. The methylesterase active site is tentatively identified as a cleft at the C-terminal edge of the beta-sheet containing residues Ser164, His190 and Asp286. The three-dimensional fold, and the arrangement of residues within the catalytic triad distinguishes the CheB methylesterase from any previously described serine protease or serine hydrolase. Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB.,West AH, Martinez-Hackert E, Stock AM J Mol Biol. 1995 Jul 7;250(2):276-90. PMID:7608974 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chemotaxis protein Methylesterase

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