Title : Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate.

Pub. Date : 2007 May 11

PMID : 17376479






5 Functional Relationships(s)
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1 However, fine regulation of CCR is accomplished by the small molecule effectors, glucose 6-phosphate (G6P) and fructose 1,6-bisphosphate (FBP), which somehow enhance CcpA-(HPr-Ser46-P) binding to DNA. 2-chloro-N(6)cyclopentyladenosine fructose-bisphosphatase 1 Homo sapiens
2 To understand the fine-tuning mechanism of these effectors, we solved the structures of the CcpA core, DeltaCcpA, which lacks the N-terminal DNA-binding domain, in complex with HPr-Ser46-P and G6P or FBP. 2-chloro-N(6)cyclopentyladenosine fructose-bisphosphatase 1 Homo sapiens
3 G6P and FBP bind in a deep cleft, between the N and C subdomains of CcpA. 2-chloro-N(6)cyclopentyladenosine fructose-bisphosphatase 1 Homo sapiens
4 Thus, stabilization of the closed conformation and bolstering of cross contacts between CcpA and its other corepressor, HPr-Ser46-P, provide a molecular explanation for how adjunct corepressors G6P and FBP enhance the interaction between CcpA-(HPr-Ser46-P) and cognate DNA. 2-chloro-N(6)cyclopentyladenosine fructose-bisphosphatase 1 Homo sapiens
5 Thus, stabilization of the closed conformation and bolstering of cross contacts between CcpA and its other corepressor, HPr-Ser46-P, provide a molecular explanation for how adjunct corepressors G6P and FBP enhance the interaction between CcpA-(HPr-Ser46-P) and cognate DNA. 2-chloro-N(6)cyclopentyladenosine fructose-bisphosphatase 1 Homo sapiens