Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase
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Title
- Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase
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Author(s)
- Cha, Sun-Shin; An, Young Jun; Jeong, Chang-Sook; Kim, Min-Kyu; Jeon, Jeong Ho; Lee, Chang-Muk; Lee, Hyun Sook; Kang, Sung Gyun; Lee, Jung-Hyun
- 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)
- 차선신; 안영준; 정창숙; 김민규; 전정호; 이현숙; 강성균; 이정현
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Publication Year
- 2013-11
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Abstract
- EstU1 is a unique family VIII carboxylesterase that displays hydrolytic activity toward the amide bond of clinically used -lactam antibiotics as well as the ester bond of p-nitrophenyl esters. EstU1 assumes a -lactamase-like modular architecture and contains the residues Ser100, Lys103, and Tyr218, which correspond to the three catalytic residues (Ser64, Lys67, and Tyr150, respectively) of class C -lactamases. The structure of the EstU1/cephalothin complex demonstrates that the active site of EstU1 is not ideally tailored to perform an efficient deacylation reaction during the hydrolysis of -lactam antibiotics. This result explains the weak -lactamase activity of EstU1 compared with class C -lactamases. Finally, structural and sequential comparison of EstU1 with other family VIII carboxylesterases elucidates an operative molecular strategy used by family VIII carboxylesterases to extend their substrate spectrum. Proteins 2013; 81:2045-2051. (c) 2013 Wiley Periodicals, Inc.
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ISSN
- 0887-3585
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/3069
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DOI
- 10.1002/prot.24334
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Bibliographic Citation
- PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.81, no.11, pp.2045 - 2051, 2013
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Publisher
- WILEY-BLACKWELL
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Subject
- TRANSITION-STATE ANALOG; BURKHOLDERIA-GLADIOLI; LIPASES; ENZYMES; CLASSIFICATION; CEPHALOSPORINS; BIOTECHNOLOGY; INHIBITION; HYDROLASE; SUBSTRATE
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Keywords
- family VIII carboxylesterases; EstU1; crystal structure of EstU1; crystal structure of the EstU1; cephalothin complex; -lactamase activity
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Type
- Article
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Language
- English
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Document Type
- Article
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