8번째 carboxylesterase family에 속하는 EstU1의 beta-lactamase 활성에 대한 구조기반 연구
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Title
- 8번째 carboxylesterase family에 속하는 EstU1의 beta-lactamase 활성에 대한 구조기반 연구
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Alternative Title
- Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase
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Author(s)
- 안영준; 정창숙; 김민규; jeong; 이현숙; 강성균; 이정현; 차선신
- KIOST Author(s)
- An, Young Jun(안영준); Lee, Hyun Sook(이현숙); Kang, Sung Gyun(강성균); Lee, Jung Hyun(이정현)
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Alternative Author(s)
- 안영준; 정창숙; 김민규; 이현숙; 강성균; 이정현; 차선신
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Publication Year
- 2013-05-03
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Abstract
- EstU1 is a remarkable family VIII carboxylesterase in that it exhibits hydrolytic activity towards the amide bond of clinically-used beta-lactam antibiotics as well as the ester bond of p-nitrophenyl esters. To reveal the structural basis for the catalytic feature, we determined the crystal structures of EstU1 and the EstU1/cephalothin complex. EstU1 assumes a two-domain structure consisting of a helical domain and a / domain. This beta-lactamase-like modular architecture, together with the fact that Ser100, Lys103, and Tyr218 in EstU1 is definitely matched with the three catalytic residues (Ser64, Lys67, and Tyr150) of class C beta-lactamases, is compatible with the beta-lactamase activity of EstU1. basis for the catalytic feature, we determined the crystal structures of EstU1 and the EstU1/cephalothin complex. EstU1 assumes a two-domain structure consisting of a helical domain and a / domain. This beta-lactamase-like modular architecture, together with the fact that Ser100, Lys103, and Tyr218 in EstU1 is definitely matched with the three catalytic residues (Ser64, Lys67, and Tyr150) of class C beta-lactamases, is compatible with the beta-lactamase activity of EstU1.
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/27095
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Bibliographic Citation
- 2013년 한국미생물학회 국제학술대회, pp.267, 2013
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Publisher
- 한국미생물학회
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Type
- Conference
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Language
- English
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