PMID: 18547145

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., [PubMed]
Sentences
No. Mutations Sentence Comment
105 ABCC8 p.Phe221Ala
X
ABCC8 p.Phe221Ala 18547145:105:5
status: NEW
view ABCC8 p.Phe221Ala details
 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. Login to comment 106 ABCC8 p.Phe221Ala
X
ABCC8 p.Phe221Ala 18547145:106:69
status: NEW
view ABCC8 p.Phe221Ala details
 A strongly decreased autokinase activity was observed with the CapAB(F221A) mutant compared to the wild-type CapAB protein (Figure S2). Login to comment 107 ABCC8 p.Phe221Ala
X
ABCC8 p.Phe221Ala 18547145:107:167
status: NEW
view ABCC8 p.Phe221Ala details
 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that this loss of activity is correlated with a reduced affinity of the CapAB(F221A) mutant for the nucleotide (unpublished data). Login to comment 273 ABCC8 p.Phe221Ala
X
ABCC8 p.Phe221Ala 18547145:273:144
status: NEW
view ABCC8 p.Phe221Ala details
 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. Login to comment