Intramolecular rearrangements as a consequence of the dephosphorylation of phosphoaspartate residues in proteins.
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.
Napper
Scott
S
Department of Biochemistry, Health Sciences Building, University of Saskatchewan, 107 Wiggins Road, Saskatoon, SK, Canada S7N 5E5.
Wolanin
Peter M
PM
Webre
Daniel J
DJ
Kindrachuk
Jason
J
Waygood
Bruce
B
Stock
Jeffry B
JB
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
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D001224:Aspartic Acid