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A kinase bioscavenger provides antibiotic resistance by extremely tight substrate binding

Kinase-mediated phosphorylation represents one of the general strategies for the emergence of antibiotic resistance. A new subfamily of AmiN-like kinases, isolated from the Siberian bear microbiome, inactivates antibiotic amicoumacin by phosphorylation. The nanomolar substrate affinity defines AmiN as a phosphotransferase with a unique catalytic efficiency proximal to the diffusion limit. Crystallographic analysis and multiscale simulations revealed a catalytically perfect mechanism providing phosphorylation exclusively in the case of a closed active site that counteracts substrate promiscuity. AmiN kinase is a member of the previously unknown subfamily representing the first evidence of a specialized phosphotransferase bioscavenger.

Grigorov Artem

Terekhov SS, Mokrushina YANazarov ASZlobin ASZalevsky AO, Bourenkov GP, Golovin AV,Belogurov AA, Osterman IA, Kulikova AA, Mitkevich VA, Hua Jane Lou, Benjamin E. Turk, Matthias Wilmanns, Smirnov IV, Sidney Altman & Gabibov AG

june 26