Document
type: Class

Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus
type: Continuant
molecularseqnum: GENBANK: CAB15441, CAB15442, CAB15642, CAB15643, CAB15441, CAB15442, CAB15642, CAB15643
type: Thing
related by: authorship_12143
related by: authorship_12141
related by: authorship_12144
related by: authorship_12142
date time value: article date 2039
related by: authorship_12151
most specific type: Article
type: Document
type: Generically Dependent Continuant
related by: authorship_12150
related by: authorship_12147
pmid: 18547145
related by: authorship_12148
artnum: e143
accesstype: All Open Access, Gold, Green
volume: 6
crisid: 2039
related by: authorship_12140
page start: 1321
doi: 10.1371/journal.pbio.0060143
estado: published
type: Entity
most specific type: Document
freetext keyword: 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
chemicalscas: 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
origen: scopus
related by: authorship_12145
related by: authorship_12146
page end: 1331
has publication venue: PLoS Biology
issue: 6
e iscopus: 2-s2.0-45849125779
type: Article
related by: authorship_12152
abstract: 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.
related by: authorship_12149
type: Information Content Entity

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type: Class

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RDF description of Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus - http://orbis.uaslp.mx/vivo/individual/scopus2038
rights: termsOfUse
date: 2026-08-26T07:20:58
publisher: vivo
type: Document

Article
type: Class

PLoS Biology
type: Journal
type: Periodical
type: Document
type: Generically Dependent Continuant
type: Thing
type: Collection
type: Continuant
type: Information Content Entity
type: Entity
publication venue for: Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus

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