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Regulatory interactions between a bacterial tyrosine kinase and its cognate phosphatase
- Source :
- Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (21), pp.15212-28. ⟨10.1074/jbc.M113.457804⟩, Journal of Biological Chemistry, 2013, 288 (21), pp.15212-28. ⟨10.1074/jbc.M113.457804⟩
- Publication Year :
- 2013
- Publisher :
- HAL CCSD, 2013.
-
Abstract
- International audience; The cyclic process of autophosphorylation of the C-terminal tyrosine cluster (YC) of a bacterial tyrosine kinase and its subsequent dephosphorylation following interactions with a counteracting tyrosine phosphatase regulates diverse physiological processes, including the biosynthesis and export of polysaccharides responsible for the formation of biofilms or virulence-determining capsules. We provide here the first detailed insight into this hitherto uncharacterized regulatory interaction at residue-specific resolution using Escherichia coli Wzc, a canonical bacterial tyrosine kinase, and its opposing tyrosine phosphatase, Wzb. The phosphatase Wzb utilizes a surface distal to the catalytic elements of the kinase, Wzc, to dock onto its catalytic domain (WzcCD). WzcCD binds in a largely YC-independent fashion near the Wzb catalytic site, inducing allosteric changes therein. YC dephosphorylation is proximity-mediated and reliant on the elevated concentration of phosphorylated YC near the Wzb active site resulting from WzcCD docking. Wzb principally recognizes the phosphate of its phosphotyrosine substrate and further stabilizes the tyrosine moiety through ring stacking interactions with a conserved active site tyrosine.
- Subjects :
- [SDV]Life Sciences [q-bio]
MESH: Catalytic Domain
MESH: Escherichia coli Proteins
Protein tyrosine phosphatase
SH2 domain
Biochemistry
MESH: Allosteric Regulation
MESH: Protein-Tyrosine Kinases
Receptor tyrosine kinase
03 medical and health sciences
Allosteric Regulation
Catalytic Domain
MESH: Phosphoprotein Phosphatases
Escherichia coli
Phosphoprotein Phosphatases
Tyrosine
Phosphotyrosine
Molecular Biology
030304 developmental biology
0303 health sciences
biology
MESH: Escherichia coli
Escherichia coli Proteins
030302 biochemistry & molecular biology
Autophosphorylation
Membrane Proteins
Cell Biology
Protein-Tyrosine Kinases
Protein Structure and Folding
biology.protein
Phosphorylation
MESH: Membrane Proteins
Tyrosine kinase
Proto-oncogene tyrosine-protein kinase Src
MESH: Phosphotyrosine
Subjects
Details
- Language :
- English
- ISSN :
- 00219258 and 1083351X
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (21), pp.15212-28. ⟨10.1074/jbc.M113.457804⟩, Journal of Biological Chemistry, 2013, 288 (21), pp.15212-28. ⟨10.1074/jbc.M113.457804⟩
- Accession number :
- edsair.doi.dedup.....772eb389e51c6cfbab7370336a020735