Structure and Function of an Unusual Family of Protein Phosphatases: The Bacterial Chemotaxis Proteins CheC and CheX
Open Access
- 19 November 2004
- journal article
- research article
- Published by Elsevier in Molecular Cell
- Vol. 16 (4) , 563-574
- https://doi.org/10.1016/j.molcel.2004.10.018
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- CheZ-Mediated Dephosphorylation of the Escherichia coli Chemotaxis Response Regulator CheY: Role for CheY Glutamate 89Journal of Bacteriology, 2003
- Structural Characterization of the Reaction Pathway in Phosphoserine Phosphatase: Crystallographic “snapshots” of Intermediate StatesJournal of Molecular Biology, 2002
- Crystal Structure of Activated CheYJournal of Biological Chemistry, 2001
- The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheYJournal of Molecular Biology, 1998
- THE TWO-COMPONENT SIGNALING PATHWAY OF BACTERIAL CHEMOTAXIS: A Molecular View of Signal Transduction by Receptors, Kinases, and Adaptation EnzymesAnnual Review of Cell and Developmental Biology, 1997
- The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras MutantsScience, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Investigating the Structural Determinants of the p21-like Triphosphate and Mg2+Binding SiteJournal of Molecular Biology, 1995
- Protein Structure Comparison by Alignment of Distance MatricesJournal of Molecular Biology, 1993
- A visual protein crystallographic software system for X11/XviewJournal of Molecular Graphics, 1992