ABCC8 p.Phe221Ala
| Predicted by SNAP2: | A: N (61%), C: N (72%), D: N (72%), E: N (57%), G: N (78%), H: N (87%), I: N (72%), K: N (61%), L: N (78%), M: N (82%), N: N (87%), P: N (53%), Q: N (82%), R: N (66%), S: N (87%), T: N (82%), V: N (78%), W: N (61%), Y: N (93%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, Q: D, R: D, S: D, T: D, V: D, W: N, Y: N, |
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[hide] Structural basis for the regulation mechanism of t... PLoS Biol. 2008 Jun 10;6(6):e143. Olivares-Illana V, Meyer P, Bechet E, Gueguen-Chaignon V, Soulat D, Lazereg-Riquier S, Mijakovic I, Deutscher J, Cozzone AJ, Laprevote O, Morera S, Grangeasse C, Nessler S
Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus.
PLoS Biol. 2008 Jun 10;6(6):e143., [PMID:18547145]
Abstract [show]
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.
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No. Sentence Comment
105 The (F221A) mutation was introduced in the CapACt segment of the chimeric CapAB protein in order to verify the essential role of residue F221a suggested by the structure.
X
ABCC8 p.Phe221Ala 18547145:105:5
status: NEW106 A strongly decreased autokinase activity was observed with the CapAB(F221A) mutant compared to the wild-type CapAB protein (Figure S2).
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ABCC8 p.Phe221Ala 18547145:106:69
status: NEW107 Preliminary fluorescence experiments using labelled nucleotide analogs further confirmed that this loss of activity is correlated with a reduced affinity of the CapAB(F221A) mutant for the nucleotide (unpublished data).
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ABCC8 p.Phe221Ala 18547145:107:167
status: NEW273 Functional Analysis of the CapA Residue F221a The autophosphorylation activity of the CapAB chimeric protein (WT) and of the F221 mutated form (F221A) was analyzed by SDS-PAGE and autoradiography.
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ABCC8 p.Phe221Ala 18547145:273:144
status: NEW