2asr

THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLITHE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI

Structural highlights 2asr is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MCP2_ECOLI Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar also mediates taxis to the attractant maltose via an interaction with the periplasmic maltose binding protein. Tar mediates taxis away from the repellents cobalt and nickel. Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Chemotaxis protein 3D structures

spinqualitylabelsall models 2asr, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image