title: Intramolecular rearrangements as a consequence of the dephosphorylation of phosphoaspartate residues in proteins.
abstract: Aspartate phosphorylation induces changes in protein conformation that are used to regulate processes ranging from gene expression and cell differentiation to cell motility and the generation of electrochemical gradients across membranes. We show here that dephosphorylation of the phosphoaspartate in the chemotaxis response regulator CheY can result in the loss of a water molecule that may be due to formation of a succinimide intermediate.
authors.affiliation: Department of Biochemistry, Health Sciences Building, University of Saskatchewan, 107 Wiggins Road, Saskatoon, SK, Canada S7N 5E5.
authors.forename: Scott
authors.initials: S
authors.lastname: Napper
authors.forename: Peter M
authors.initials: PM
authors.lastname: Wolanin
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Webre
authors.forename: Jason
authors.initials: J
authors.lastname: Kindrachuk
authors.forename: Bruce
authors.initials: B
authors.lastname: Waygood
authors.forename: Jeffry B
authors.initials: JB
authors.lastname: Stock
mesh_terms: D001224:Aspartic Acid / Q000737:chemistry / Q000378:metabolism*; D001426:Bacterial Proteins; D013058:Mass Spectrometry; D008565:Membrane Proteins / Q000737:chemistry*; D000072236:Methyl-Accepting Chemotaxis Proteins; D010766:Phosphorylation
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D001224:Aspartic Acid