High mobility of carboxyl-terminal region of bacterial chemotaxis phosphatase CheZ is diminished upon binding divalent cation or CheY-P substrate.

Silversmith, Ruth E

High mobility of carboxyl-terminal region of bacterial chemotaxis phosphatase CheZ is diminished upon binding divalent cation or CheY-P substrate. [electronic resource] - Biochemistry May 2005 - 7768-76 p. digital

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.

0006-2960

10.1021/bi0501636 doi


Amino Acid Sequence
Bacterial Proteins--antagonists & inhibitors
Beryllium--metabolism
Binding Sites
Cations, Divalent--chemistry
Chemotaxis
Escherichia coli Proteins
Fluorescein--metabolism
Fluorescence Polarization
Fluorescence Resonance Energy Transfer
Fluorides--metabolism
Magnesium Chloride--chemistry
Membrane Proteins--antagonists & inhibitors
Methyl-Accepting Chemotaxis Proteins
Molecular Motor Proteins--antagonists & inhibitors
Molecular Sequence Data
Peptide Fragments--antagonists & inhibitors
Phosphoric Monoester Hydrolases--antagonists & inhibitors
Protein Structure, Tertiary
Substrate Specificity