Document
cap binding protein; polysaccharide; protein CapA; protein tyrosine kinase; protein tyrosine kinase CapB; bacterial protein; Escherichia coli protein; membrane protein; nucleotide; protein tyrosine kinase; wzc protein, E coli; article; bacterial virulence; crystal structure; enzyme phosphorylation; enzyme regulation; enzyme structure; eukaryote; nonhuman; nucleotide sequence; protein domain; protein function; protein phosphorylation; regulatory mechanism; Staphylococcus aureus; transcription initiation site; binding site; biological model; chemical structure; chemistry; comparative study; enzymology; metabolism; molecular genetics; phosphorylation; protein tertiary structure; X ray crystallography; Bacteria (microorganisms); Eukaryota; Staphylococcus aureus; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Escherichia coli Proteins; Membrane Proteins; Models, Biological; Models, Molecular; Molecular Sequence Data; Nucleotides; Phosphorylation; Protein Structure, Tertiary; Protein-Tyrosine Kinases; Staphylococcus aureus
protein tyrosine kinase, 80449-02-1; Bacterial Proteins; Escherichia coli Proteins; Membrane Proteins; Nucleotides; Protein-Tyrosine Kinases, 2.7.10.1; wzc protein, E coli, 2.7.10.2
Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus
Bacteria were thought to be devoid of tyrosine-phosphorylating enzymes. However, several tyrosine kinases without similarity to their eukaryotic counterparts have recently been identified in bacteria. They are involved in many physiological processes, but their accurate functions remain poorly understood due to slow progress in their structural characterization. They have been best characterized as copolymerases involved in the synthesis and export of extracellular polysaccharides. These compounds play critical roles in the virulence of pathogenic bacteria, and bacterial tyrosine kinases can thus be considered as potential therapeutic targets. Here, we present the crystal structures of the phosphorylated and unphosphorylated states of the tyrosine kinase CapB from the human pathogen Staphylococcus aureus together with the activator domain of its cognate transmembrane modulator CapA. This first high-resolution structure of a bacterial tyrosine kinase reveals a 230-kDa ring-shaped octamer that dissociates upon intermolecular autophosphorylation. These observations provide a molecular basis for the regulation mechanism of the bacterial tyrosine kinases and give insights into their copolymerase function. © 2008 Olivares-Illana et al.
Generically Dependent Continuant
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