4H05

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

4H05 の概要

• エントリーDOI: 10.2210/pdb4h05/pdb
• 分子名称: Aminoglycoside-O-phosphotransferase VIII (2 entities in total)
• 機能のキーワード: protein kinase, atp binding, aminoglycoside phosphotransferase viii; aminoglycoside antibiotic, phosphorilation, transferase
• 由来する生物種: Streptomyces rimosus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60143.66

構造登録者

Boyko, K.M.,Gorbacheva, M.A.,Danilenko, V.N.,Alekseeva, M.G.,Korzhenevskiy, D.A.,Dorovatovskiy, P.V.,Lipkin, A.V.,Popov, V.O. (登録日: 2012-09-07, 公開日: 2014-04-09, 最終更新日: 2023-09-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.15 Å)