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 under...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2008-06-01
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| Series: | PLoS Biology |
| Online Access: | http://europepmc.org/articles/PMC2422856?pdf=render |
| _version_ | 1818887316026949632 |
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| author | Vanesa Olivares-Illana Philippe Meyer Emmanuelle Bechet Virginie Gueguen-Chaignon Didier Soulat Sylvie Lazereg-Riquier Ivan Mijakovic Josef Deutscher Alain J Cozzone Olivier Laprévote Solange Morera Christophe Grangeasse Sylvie Nessler |
| author_facet | Vanesa Olivares-Illana Philippe Meyer Emmanuelle Bechet Virginie Gueguen-Chaignon Didier Soulat Sylvie Lazereg-Riquier Ivan Mijakovic Josef Deutscher Alain J Cozzone Olivier Laprévote Solange Morera Christophe Grangeasse Sylvie Nessler |
| author_sort | Vanesa Olivares-Illana |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-19T16:35:17Z |
| format | Article |
| id | doaj.art-0389812f019f4d8c938d70a3a0b7d8e6 |
| institution | Directory Open Access Journal |
| issn | 1544-9173 1545-7885 |
| language | English |
| last_indexed | 2024-12-19T16:35:17Z |
| publishDate | 2008-06-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Biology |
| spelling | doaj.art-0389812f019f4d8c938d70a3a0b7d8e62022-12-21T20:13:59ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852008-06-0166e14310.1371/journal.pbio.0060143Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus.Vanesa Olivares-IllanaPhilippe MeyerEmmanuelle BechetVirginie Gueguen-ChaignonDidier SoulatSylvie Lazereg-RiquierIvan MijakovicJosef DeutscherAlain J CozzoneOlivier LaprévoteSolange MoreraChristophe GrangeasseSylvie NesslerBacteria 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.http://europepmc.org/articles/PMC2422856?pdf=render |
| spellingShingle | Vanesa Olivares-Illana Philippe Meyer Emmanuelle Bechet Virginie Gueguen-Chaignon Didier Soulat Sylvie Lazereg-Riquier Ivan Mijakovic Josef Deutscher Alain J Cozzone Olivier Laprévote Solange Morera Christophe Grangeasse Sylvie Nessler Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus. PLoS Biology |
| title | Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus. |
| title_full | Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus. |
| title_fullStr | Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus. |
| title_full_unstemmed | Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus. |
| title_short | Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus. |
| title_sort | structural basis for the regulation mechanism of the tyrosine kinase capb from staphylococcus aureus |
| url | http://europepmc.org/articles/PMC2422856?pdf=render |
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