Preparation, crystallization and preliminary X-ray crystallographic analysis of OXA-23, a carbapenemase conferring widespread antibiotic resistance.
Indian J Biochem Biophys
;
2011 Dec; 48(6): 395-398
Article
in English
| IMSEAR
| ID: sea-140206
ABSTRACT
OXA-23, a class D carbapenemase that confers widespread antibiotic resistance hydrolyzes the β-lactam rings of β-lactam antibiotics, presenting an enormous challenge to infection control, particularly in the eradication of pathogenic bacteria such as Acinetobacter baumannii, one of six top-priority dangerous pathogens. Thus, the enzyme is a potential target for developing antimicrobial agents against pathogens producing carbapenemases. In this study, OXA-23 was purified and crystallized at 298 K and X-ray diffraction data from OXA-23 crystal were collected at 2.03 Å resolution using synchrotron radiation. The crystal of OXA-23 belonged to space group P41 with unit cell parameters a = 82.47, b = 82.47 and c = 172.01 Å. Analysis of the packing density showed that the asymmetric unit probably contained two molecules with a solvent content of 73.64%.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Beta-Lactamases
/
Drug Resistance, Microbial
/
Molecular Sequence Data
/
Amino Acid Sequence
/
Sequence Homology, Amino Acid
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Crystallography, X-Ray
/
Crystallization
/
Electrophoresis, Polyacrylamide Gel
Language:
English
Journal:
Indian J Biochem Biophys
Year:
2011
Type:
Article
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