Interdomain interaction of cyclic AMP receptor protein in the absence of cyclic AMP.
Interdomain interaction of apo-cyclic AMP receptor protein (apo-CRP) was qualified using its isolated domains. The cAMP-binding domain was prepared by a limited proteolysis, while the DNA-binding domain was constructed as a recombinant protein. Three different regions making interdomain contacts in apo-CRP were identified by a sequence-specific comparison of the HSQC spectra. The results indicated that apo-CRP possesses characteristic modules of interdomain interaction that are properly organized to suppress activity and to sense and transfer the cAMP binding signals. Particularly, the inertness of the DNA-binding motif in apo-CRP was attributable to the participation of F-helices in the interdomain contacts.
Won
Hyung-Sik
HS
Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk, Korea. wonhs@kku.ac.kr
Seo
Min-Duk
MD
Ko
Hyun-Suk
HS
Choi
Wahn Soo
WS
Lee
Bong-Jin
BJ
D001665:Binding Sites; D000242:Cyclic AMP / Q000378:metabolism*; D002373:Cyclic AMP Receptor Protein / Q000378:metabolism*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular
D002373:Cyclic AMP Receptor Protein; D000242:Cyclic AMP