Earticle

초록

영어

β-Lactam antibiotics such as penicillins and cephalosporins have a four-atomring as a common element in their structure. The β- lactamases, which catalyze the inactivation of these ntibiotics, are of great interest because of their high incidence in pathogenic bacteria. A novel oligomeric class C β-lactamase (Est-Y29) from a metagenomic library was expressed, purified and crystallized. Est-Y29 possesses the Ser-X-X-Lys motif which is highly conserved among β-lactamases and site-directed mutagenesis of Ser to Ala resulted in complete loss of activity(1). To our knowledge, Est-Y29 is the first multimeric class C β-lactamase with broad hydrolytic activity. The recombinant protein was expressed in Escherichia coli with an N-terminal 6×His tag and purified to homogeneity. EstY-29 was crystallized and X-ray intensity data were collected to 1.49 A ° resolution using synchrotron radiation. The crystal structure of Est-Y29 will provide an invaluable framework for understanding its unique features such as its oligomeric state, high stability and (S)-specific stereoselectivity, as well as its significance for the development of antibiotic drugs against class C β-lactamases.

키워드

저자

• Sang Chul KIM [ Department of Molecular Science and Technology, Ajou University ]
• Seung Bum KIM [ Department of Molecular Science and Technology, Ajou University ]
• Sung Soo KIM [ Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon. ]
• Kyeong Kyu KIM [ Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon. ]
• Yeon Woo RYU [ Department of Molecular Science and Technology, Ajou University ]
• T. Doohun KIM [ Department of Molecular Science and Technology, Ajou University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576