Title : Escherichia coli cAMP receptor protein: evidence for three protein conformational states with different promoter binding affinities.

Pub. Date : 1989 Aug 22

PMID : 2554959






6 Functional Relationships(s)
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1 The association constants for the formation of CRP-cAMP and CRP-(cAMP)2 complexes derived from conformational studies are in good agreement with those determined by equilibrium dialysis, nonequilibrium dialysis, and ultrafiltration. Cyclic AMP catabolite gene activator protein Escherichia coli
2 Therefore, the simplest explanation would be that the protein exhibits three conformational states, free CRP and two cAMP-dependent states, which correspond to the CRP-cAMP and CRP-(cAMP)2 complexes. Cyclic AMP catabolite gene activator protein Escherichia coli
3 Therefore, the simplest explanation would be that the protein exhibits three conformational states, free CRP and two cAMP-dependent states, which correspond to the CRP-cAMP and CRP-(cAMP)2 complexes. Cyclic AMP catabolite gene activator protein Escherichia coli
4 Therefore, the simplest explanation would be that the protein exhibits three conformational states, free CRP and two cAMP-dependent states, which correspond to the CRP-cAMP and CRP-(cAMP)2 complexes. Cyclic AMP catabolite gene activator protein Escherichia coli
5 At a high concentration of cAMP which favors the formation of the CRP-(cAMP)2 complex, binding of the protein to DNA is decreased. Cyclic AMP catabolite gene activator protein Escherichia coli
6 This, together with conformational data, strongly suggests that only the CRP-cAMP complex is active in specific DNA binding whereas CRP and CRP-(cAMP)2 are not. Cyclic AMP catabolite gene activator protein Escherichia coli