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Rogne P, Andersson D, Grundström C, Sauer-Eriksson E, Linusson A, Wolf-Watz M
Biochemistry 58 (32) 3408-3412 [2019-08-13; online 2019-07-29]
As a key molecule in biology, adenosine triphosphate (ATP) has numerous crucial functions in, for instance, energetics, post-translational modifications, nucleotide biosynthesis, and cofactor metabolism. Here, we have discovered an intricate interplay between the enzyme adenylate kinase and its substrate ATP. The side chain of an arginine residue was found to be an efficient sensor of the aromatic moiety of ATP through the formation of a strong cation-π interaction. In addition to recognition, the interaction was found to have dual functionality. First, it nucleates the activating conformational transition of the ATP binding domain and also affects the specificity in the distant AMP binding domain. In light of the functional consequences resulting from the cation-π interaction, it is possible that the mode of ATP recognition may be a useful tool in enzyme design.
Swedish NMR Centre (SNC) [Service]
PubMed 31339702
DOI 10.1021/acs.biochem.9b00538
Crossref 10.1021/acs.biochem.9b00538