Intramolecular rearrangements as a consequence of the dephosphorylation of phosphoaspartate residues in proteins
Open Access
- 12 February 2003
- journal article
- Published by Wiley in FEBS Letters
- Vol. 538 (1-3) , 77-80
- https://doi.org/10.1016/s0014-5793(03)00132-7
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.Keywords
This publication has 16 references indexed in Scilit:
- Two-Component Signal TransductionAnnual Review of Biochemistry, 2000
- NMR structure of activated CheYJournal of Molecular Biology, 2000
- Reaction Mechanism of Fluoroacetate Dehalogenase from Moraxella sp. BJournal of Biological Chemistry, 1998
- A Source of Response Regulator Autophosphatase Activity: The Critical Role of a Residue Adjacent to the Spo0F Autophosphorylation Active SiteBiochemistry, 1998
- Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli.Proceedings of the National Academy of Sciences, 1995
- Reaction Mechanism of L-2-Haloacid Dehalogenase of Pseudomonas sp. YLPublished by Elsevier ,1995
- Structure of the magnesium-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxisBiochemistry, 1993
- Signal transduction in bacteriaNature, 1990
- Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxisCell, 1988
- Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteinsInternational Journal of Peptide and Protein Research, 1987