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FEBS Lett. 2017 Apr;591(7):1064-1070. doi: 10.1002/1873-3468.12613. Epub 2017 Mar 19.

C-terminal dimerization of apo-cyclic AMP receptor protein validated in solution.

Author information

1
Department of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk, Korea.
2
Protein Structure Group, Korea Basic Science Institute, Ochang, Chungbuk, Korea.
3
Department of Molecular Science and Technology, Ajou University, Suwon, Gyeonggi, Korea.
4
Research Institute of Pharmaceutical Science and Technology, College of Pharmacy, Ajou University, Suwon, Gyeonggi, Korea.
5
College of Pharmacy, Korea University, Sejong, Korea.
6
Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
7
Department of Bio-Engineering, Life Science RD Center, Sinil Pharmaceutical Co., Seongnam, Gyeonggi, Korea.

Abstract

Although cyclic AMP receptor protein (CRP) has long served as a typical example of effector-mediated protein allostery, mechanistic details into its regulation have been controversial due to discrepancy between the known crystal structure and NMR structure of apo-CRP. Here, we report that the recombinant protein corresponding to its C-terminal DNA-binding domain (CDD) forms a dimer. This result, together with structural information obtained in the present NMR study, is consistent with the previous crystal structure and validates its relevance also in solution. Therefore, our findings suggest that dissociation of the CDD may be critically involved in cAMP-induced allosteric activation of CRP.

KEYWORDS:

NMR spectroscopy; cyclic AMP receptor protein; protein allostery

PMID:
28245055
DOI:
10.1002/1873-3468.12613
[Indexed for MEDLINE]
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