Expression, purification, crystallization, and preliminary X-ray crystallographic analysis of OXA-17, an extended-spectrum {beta}-lactamase conferring severe antibiotic resistance
- Myongji University, Drug Resistance Proteomics Laboratory, Department of Biological Sciences (Korea, Republic of)
OXA-17, an extended-spectrum {beta}-lactamase (ESBL) conferring severe antibiotic resistance, hydrolytically inactivates {beta}-lactam antibiotics, inducing a lack of eradication of pathogenic bacteria by oxyimino {beta}-lactams and not helping hospital infection control. Thus, the enzyme is a potential target for developing antimicrobial agents against pathogens producing ESBLs. OXA-17 was purified and crystallized at 298 K. X-ray diffraction data from OXA-17 crystal have been collected to 1.85 A resolution using synchrotron radiation. The crystal of OXA-17 belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 48.37, b = 101.12, and c = 126.07 A. Analysis of the packing density shows that the asymmetric unit probably contains two molecules with a solvent content of 54.6%.
- OSTI ID:
- 22121687
- Journal Information:
- Crystallography Reports, Vol. 58, Issue 4; Other Information: Copyright (c) 2013 Pleiades Publishing, Ltd.; http://www.springer-ny.com; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
SUPERCONDUCTIVITY AND SUPERFLUIDITY
ANTIBIOTICS
ANTIMICROBIAL AGENTS
ASYMMETRY
BACTERIA
CRYSTALLIZATION
CRYSTALLOGRAPHY
CRYSTALS
ENZYMES
LACTAMS
ORTHORHOMBIC LATTICES
PATHOGENS
PURIFICATION
RESOLUTION
SOLVENTS
SPACE GROUPS
SYNCHROTRON RADIATION
TEMPERATURE RANGE 0273-0400 K
X RADIATION
X-RAY DIFFRACTION