Download MendeleyStructural characterization of the novel aminoglycoside phosphotransferase AphVIII from Streptomyces rimosus with enzymatic activity modulated by phosphorylation.
Boyko, K.M., Gorbacheva, M.A., Korzhenevskiy, D.A., Alekseeva, M.G., Mavletova, D.A., Zakharevich, N.V., Elizarov, S.M., Rudakova, N.N., Danilenko, V.N., Popov, V.O.(2016) Biochem Biophys Res Commun 477: 595-601
- PubMed: 27338640
- DOI: https://doi.org/10.1016/j.bbrc.2016.06.097
- Primary Citation of Related Structures:
4H05 - PubMed Abstract:
Aminoglycoside phosphotransferases represent a broad class of enzymes that promote bacterial resistance to aminoglycoside antibiotics via the phosphorylation of hydroxyl groups in the latter. Here we report the spatial structure of the 3'-aminoglycoside phosphotransferase of novel VIII class (AphVIII) solved by X-ray diffraction method with a resolution of 2.15 Å. Deep analysis of APHVIII structure and its comparison with known structures of aminoglycoside phosphotransferases of various types reveals that AphVIII has a typical two-domain fold and, however, possesses some unique characteristics that distinguish the enzyme from its known homologues. The most important difference is the presence of the activation loop with unique Ser146 residue. We demonstrate that in the apo-state of the enzyme the activation loop does not interact with other parts of the enzyme and seems to adopt catalytically competent state only after substrate binding.
Organizational Affiliation:
Bach Institute of Biochemistry, Federal Research Centre of Biotechnology of the Russian Academy of Sciences, Leninsky Prospekt. 33, Bld. 2, 119071, Moscow, Russian Federation; National Research Center "Kurchatov Institute", Kurchatov Complex of NBICS-technologies, Akad. Kurchatova sqr., 1, Moscow, 123182, Russian Federation. Electronic address: kmb@inbi.ras.ru.
