6SV5

Amicoumacin kinase AmiN in complex with ATP

Summary for 6SV5

• Entry DOI: 10.2210/pdb6sv5/pdb
• Descriptor: Phosphotransferase enzyme family protein, amicoumacin kinase, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: antimicrobial protein, kinase, amicoumacin
• Biological source: Bacillus pumilus
• Total number of polymer chains: 1
• Total formula weight: 39618.18

Authors

Bourenkov, G.P.,Mokrushina, Y.A.,Terekhov, S.S.,Smirnov, I.V.,Gabibov, A.G.,Altman, S. (deposition date: 2019-09-17, release date: 2020-07-22, Last modification date: 2024-05-15)

Primary citation

Terekhov, S.S.,Mokrushina, Y.A.,Nazarov, A.S.,Zlobin, A.,Zalevsky, A.,Bourenkov, G.,Golovin, A.,Belogurov Jr., A.,Osterman, I.A.,Kulikova, A.A.,Mitkevich, V.A.,Lou, H.J.,Turk, B.E.,Wilmanns, M.,Smirnov, I.V.,Altman, S.,Gabibov, A.G.
A kinase bioscavenger provides antibiotic resistance by extremely tight substrate binding.
Sci Adv, 6:eaaz9861-eaaz9861, 2020

PubMed 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.

PubMed: 32637600
DOI: 10.1126/sciadv.aaz9861

Experimental method

X-RAY DIFFRACTION (2 Å)