4h05

Publication Abstract from PubMed

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 A. 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.

Structural characterization of the novel aminoglycoside phosphotransferase AphVIII from Streptomyces rimosus with enzymatic activity modulated by phosphorylation.,Boyko KM, Gorbacheva MA, Korzhenevskiy DA, Alekseeva MG, Mavletova DA, Zakharevich NV, Elizarov SM, Rudakova NN, Danilenko VN, Popov VO Biochem Biophys Res Commun. 2016 Sep 2;477(4):595-601. doi:, 10.1016/j.bbrc.2016.06.097. Epub 2016 Jun 20. PMID:27338640^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.