6SUN
Amicoumacin kinase hAmiN in complex with AMP-PNP, Ca2+ and Ami
Summary for 6SUN
| Entry DOI | 10.2210/pdb6sun/pdb |
| Descriptor | APH domain-containing protein, amicoumacin kinase, CALCIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total) |
| Functional Keywords | antimicrobial protein, kinase, amicoumacin |
| Biological source | Bacillus pumilus |
| Total number of polymer chains | 1 |
| Total formula weight | 40527.57 |
| Authors | Bourenkov, G.P.,Mokrushina, Y.A.,Terekhov, S.S.,Smirnov, I.V.,Gabibov, A.G.,Altman, S. (deposition date: 2019-09-16, 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 Cited by 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: 32637600DOI: 10.1126/sciadv.aaz9861 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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