6B9B

Crystal structure of the catalase-peroxidase from B. pseudomallei with maltose bound

6B9B の概要

• エントリーDOI: 10.2210/pdb6b9b/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Catalase-peroxidase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, PROTOPORPHYRIN IX CONTAINING FE, ... (9 entities in total)
• 機能のキーワード: catalase, peroxidase, maltose, heme, oxidoreductase
• 由来する生物種: Burkholderia pseudomallei 1710b
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 161780.88

構造登録者

Loewen, P.C. (登録日: 2017-10-10, 公開日: 2018-07-04, 最終更新日: 2023-11-15)

主引用文献

Loewen, P.C.,De Silva, P.M.,Donald, L.J.,Switala, J.,Villanueva, J.,Fita, I.,Kumar, A.
KatG-Mediated Oxidation Leading to Reduced Susceptibility of Bacteria to Kanamycin.
ACS Omega, 3:4213-4219, 2018

PubMed Abstract: Resistance to antibiotics has become a serious problem for society, and there are increasing efforts to understand the reasons for and sources of resistance. Bacterial-encoded enzymes and transport systems, both innate and acquired, are the most frequent culprits for the development of resistance, although in , the catalase-peroxidase, KatG, has been linked to the activation of the antitubercular drug isoniazid. While investigating a possible link between aminoglycoside antibiotics and the induction of oxidative bursts, we observed that KatG reduces susceptibility to aminoglycosides. Investigation revealed that kanamycin served as an electron donor for the peroxidase reaction, reducing the oxidized ferryl intermediates of KatG to the resting state. Loss of electrons from kanamycin was accompanied by the addition of a single oxygen atom to the aminoglycoside. The oxidized form of kanamycin proved to be less effective as an antibiotic. Kanamycin inhibited the crystallization of KatG, but the smaller, structurally related glycoside maltose did cocrystallize with KatG, providing a suggestion as to the possible binding site of kanamycin.

PubMed: 29732452
DOI: 10.1021/acsomega.8b00356

実験手法

X-RAY DIFFRACTION (1.8 Å)