6B9B

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

Summary for 6B9B

• Entry DOI: 10.2210/pdb6b9b/pdb
• Related PRD ID: PRD_900001
• Descriptor: Catalase-peroxidase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, PROTOPORPHYRIN IX CONTAINING FE, ... (9 entities in total)
• Functional Keywords: catalase, peroxidase, maltose, heme, oxidoreductase
• Biological source: Burkholderia pseudomallei 1710b
• Total number of polymer chains: 2
• Total formula weight: 161780.88

Authors

Loewen, P.C. (deposition date: 2017-10-10, release date: 2018-07-04, Last modification date: 2023-11-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)