Abstract:
:Microbial communities are self-controlled by repertoires of lethal agents, the antibiotics. In their turn, these antibiotics are regulated by bioscavengers that are selected in the course of evolution. 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.
journal_name
Sci Advjournal_title
Science advancesauthors
Terekhov SS,Mokrushina YA,Nazarov AS,Zlobin A,Zalevsky A,Bourenkov G,Golovin A,Belogurov A Jr,Osterman IA,Kulikova AA,Mitkevich VA,Lou HJ,Turk BE,Wilmanns M,Smirnov IV,Altman S,Gabibov AGdoi
10.1126/sciadv.aaz9861subject
Has Abstractpub_date
2020-06-24 00:00:00pages
eaaz9861issue
26issn
2375-2548pii
aaz9861journal_volume
6pub_type
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