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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Crystallization and preliminary X-ray crystallographic analyses of CMY-1 and CMY-10, plasmidic class C beta-lactamases with extended substrate spectrum

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Title
Crystallization and preliminary X-ray crystallographic analyses of CMY-1 and CMY-10, plasmidic class C beta-lactamases with extended substrate spectrum
Author
Lee, SJKim, JYJung, HISuh, Pann-GhillLee, HSLee, SHCha, SS
Issue Date
2004-02
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.60, no.2, pp.382 - 384
Abstract
Plasmid-encoded class C β-lactamases, including CMY-1 and CMY-10, hydrolyze the lactam bonds of β-lactam antibiotics, inducing therapeutic failure and a lack of eradication of clinical isolates by third-generation cephalosporins or cephamycins. Therefore, the enzymes are potential targets for developing agents against pathogens isolated from patients suffering from wound infection, urinary tract infection or pneumonia. CMY-1 and CMY-10 were purified and crystallized at 298 K. X-ray diffraction data from CMY-1 and CMY-10 crystals have been collected to 2.5 and 1.5 A resolution, respectively, using synchrotron radiation. The crystals of the two proteins are isomorphous and belong to the primitive monoclinic space group P21.
URI
https://scholarworks.unist.ac.kr/handle/201301/5612
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=4644281606
DOI
10.1107/S090744490302821X
ISSN
0907-4449
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