A kinase bioscavenger provides antibiotic resistance by extremely tight substrate binding

Author:

Terekhov Stanislav S.12ORCID,Mokrushina Yuliana A.12ORCID,Nazarov Anton S.1ORCID,Zlobin Alexander13ORCID,Zalevsky Arthur134ORCID,Bourenkov Gleb5ORCID,Golovin Andrey134ORCID,Belogurov Alexey1,Osterman Ilya A.26,Kulikova Alexandra A.7ORCID,Mitkevich Vladimir A.7ORCID,Lou Hua Jane8,Turk Benjamin E.8,Wilmanns Matthias5,Smirnov Ivan V.12ORCID,Altman Sidney910ORCID,Gabibov Alexander G.1211ORCID

Affiliation:

1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, Russia.

2. Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.

3. Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia.

4. Sechenov First Moscow State Medical University, Institute of Molecular Medicine, Moscow, Russia.

5. European Molecular Biology Laboratory, Hamburg, Germany.

6. Skolkovo Institute of Science and Technology, Skolkovo, Russia.

7. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.

8. Department of Pharmacology, Yale School of Medicine, New Haven, CT, USA.

9. Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT, USA.

10. Arizona State University, Tempe, AZ, USA.

11. Department of Life Sciences, Higher School of Economics, Moscow, Russia.

Abstract

The substrate-driven closure determines an outstanding efficacy of antibiotic inactivation in a new kinase subfamily.

Funder

National Institutes of Health

Russian Foundation for Basic Research

Russian Science Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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