4H05

Crystal structure of aminoglycoside-3'-phosphotransferase of type VIII

Summary for 4H05

• Entry DOI: 10.2210/pdb4h05/pdb
• Descriptor: Aminoglycoside-O-phosphotransferase VIII (2 entities in total)
• Functional Keywords: protein kinase, atp binding, aminoglycoside phosphotransferase viii; aminoglycoside antibiotic, phosphorilation, transferase
• Biological source: Streptomyces rimosus
• Total number of polymer chains: 2
• Total formula weight: 60143.66

Authors

Boyko, K.M.,Gorbacheva, M.A.,Danilenko, V.N.,Alekseeva, M.G.,Korzhenevskiy, D.A.,Dorovatovskiy, P.V.,Lipkin, A.V.,Popov, V.O. (deposition date: 2012-09-07, release date: 2014-04-09, Last modification date: 2023-09-13)

Primary citation

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.
Structural characterization of the novel aminoglycoside phosphotransferase AphVIII from Streptomyces rimosus with enzymatic activity modulated by phosphorylation.
Biochem.Biophys.Res.Commun., 477:595-601, 2016

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.

PubMed: 27338640
DOI: 10.1016/j.bbrc.2016.06.097

Experimental method

X-RAY DIFFRACTION (2.15 Å)