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Intramolecular rearrangements as a consequence of the dephosphorylation of phosphoaspartate residues in proteins
Author(s) -
Napper Scott,
Wolanin Peter M.,
Webre Daniel J.,
Kindrachuk Jason,
Waygood Bruce,
Stock Jeffry B.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00132-7
Subject(s) - dephosphorylation , phosphorylation , chemotaxis , regulator , succinimide , chemistry , intramolecular force , motility , microbiology and biotechnology , biophysics , membrane , biochemistry , stereochemistry , biology , gene , receptor , phosphatase
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.