Article
Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.1-A structure of a threonine to isoleucine mutant at position 87 of CheY.
The Journal of biological chemistry - 21 Jul 1995
Ganguli S, Wang H, Matsumura P, Volz K
Abstract excerpt
Position 87 of the chemotaxis regulatory protein CheY is a highly conserved threonine/serine residue in the response regulator superfamily. A threonine 87 to isoleucine mutant in CheY, identified by its in vivo non-chemotactic phenotype, was also found to be phosphorylatable in vitro. These properties indicate that this mutant does not undergo activation upon phosphorylation. The x-ray crystallographic structure...
Topics
- Bacterial Proteins
- Binding Sites
- Chemotactic Factors
- Crystallography, X-Ray
- Isoleucine
- Membrane Proteins
- Methyl-Accepting Chemotaxis Proteins
- Mutation
- Phosphorylation
- Protein Conformation