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• W2137338081 startingPage "6793" @default.
• W2137338081 abstract "In Gram-positive bacteria, the catabolite control protein A (CcpA) functions as the master transcriptional regulator of carbon catabolite repression/regulation (CCR). To effect CCR, CcpA binds a phosphoprotein, either HPr-Ser⁴⁶-P or Crh-Ser⁴⁶-P. Although Crh and histidine-containing protein (HPr) are structurally homologous, CcpA binds Crh-Ser⁴⁶-P more weakly than HPr-Ser⁴⁶-P. Moreover, Crh can form domain-swapped dimers, which have been hypothesized to be functionally relevant in CCR. To understand the molecular mechanism of Crh-Ser⁴⁶-P regulation of CCR, we determined the structure of a CcpA-(Crh-Ser⁴⁶-P)-DNA complex. The structure reveals that Crh-Ser⁴⁶-P does not bind CcpA as a dimer but rather interacts with CcpA as a monomer in a manner similar to that of HPr-Ser⁴⁶-P. The reduced affinity of Crh-Ser⁴⁶-P for CcpA as compared with that of HPr-Ser⁴⁶ P is explained by weaker Crh-Ser⁴⁶-P interactions in its contact region I to CcpA, which causes this region to shift away from CcpA. Nonetheless, the interface between CcpA and helix α 2 of the second contact region (contact region II) of Crh-Ser⁴⁶-P is maintained. This latter finding demonstrates that this contact region is necessary and sufficient to throw the allosteric switch to activate <i>cre</i> binding by CcpA." @default.
• W2137338081 created "2016-06-24" @default.
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• W2137338081 date "2006-03-01" @default.
• W2137338081 modified "2023-10-13" @default.
• W2137338081 title "Phosphoprotein Crh-Ser46-P Displays Altered Binding to CcpA to Effect Carbon Catabolite Regulation" @default.
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• W2137338081 doi "https://doi.org/10.1074/jbc.m509977200" @default.
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