Crystallization and Preliminary X-Ray Crystallographic Analysis of CTX-M-15, an Extended-spectrum beta-Lactamase Conferring Worldwide Emerging Antibiotic Resistance
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Title
- Crystallization and Preliminary X-Ray Crystallographic Analysis of CTX-M-15, an Extended-spectrum beta-Lactamase Conferring Worldwide Emerging Antibiotic Resistance
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Author(s)
- An, Young Jun; Lee, Jung Hun; Jung, Ha Il; Sohn, Seung Ghyu; Lee, Jae Jin; Park, Kwang Seung; Wu, Xing; Jeong, Byeong Chul; Kang, Choong-Min; Cha, Sun-Shin; Lee, Sang Hee
- KIOST Author(s)
- An, Young Jun(안영준)
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Alternative Author(s)
- 안영준; 차선신
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Publication Year
- 2011-09
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Abstract
- CTX-M-15, an extended-spectrum beta-lactamase emerging worldwide, hydrolyzes lactam ring of beta-lactam antibiotics, and thus causes therapeutic failure and a lack of eradication of pathogenic bacteria by third-generation beta-lactams. Therefore, the enzyme is a potential target for developing agents against pathogens isolated from patients suffering from nosocomial infections. The CTX-M-15 protein was purified and crystallized at 298 K. X-ray diffraction data from CTX-M-15 crystal have been collected to 1.46 angstrom resolution using synchrotron radiation. The crystal of CTX-M-15 belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 45.50, b = 44.23, and c = 116.92 angstrom. Analysis of the packing density shows that the asymmetric unit probably contains two molecules with a solvent content of 41.26%.
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ISSN
- 0929-8665
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/3820
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DOI
- 10.2174/092986611796011400
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Bibliographic Citation
- PROTEIN AND PEPTIDE LETTERS, v.18, no.9, pp.858 - 862, 2011
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Publisher
- BENTHAM SCIENCE PUBL LTD
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Subject
- CTX-M ENZYMES; SUBSTITUTION; CEFTAZIDIME; EFFICIENCY
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Keywords
- Antibiotic resistance; cefotaxime; ceftazidime; crystal; CTX-M-15; extended-spectrum beta-lactamase
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Type
- Article
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Language
- English
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Document Type
- Article
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