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C‐terminal dimerization of apo‐cyclic AMP receptor protein validated in solution
Author(s) -
Sim DaeWon,
Choi Jae Wan,
Kim JiHun,
Ryu KyoungSeok,
Kim Myeongkyu,
Yu HeeWan,
Jo KuSung,
Kim EunHee,
Seo MinDuk,
Jeon Young Ho,
Lee BongJin,
Kim Young Pil,
Won HyungSik
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12613
Subject(s) - allosteric regulation , dimer , chemistry , recombinant dna , crystal structure , effector , receptor , dissociation (chemistry) , protein structure , biophysics , stereochemistry , biochemistry , crystallography , biology , gene , organic chemistry
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 .