Crystal structure of EstSRT1, a family VIII carboxylesterase displaying hydrolytic activity toward oxyimino cephalosporins
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Title
- Crystal structure of EstSRT1, a family VIII carboxylesterase displaying hydrolytic activity toward oxyimino cephalosporins
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Author(s)
- Cha, Sun-Shin; An, Young Jun
- KIOST Author(s)
- An, Young Jun(안영준)
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Alternative Author(s)
- 안영준
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Publication Year
- 2016-09-16
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Abstract
- EstSRT1 is a family VIII carboxylesterase that hydrolyzes oxyimino third- and fourth-generation cephalosporins, first-generation cephalosporins and ester substrates. According to the crystal structure of EstSRT1 (2.0-angstrom resolution), this protein contains a large alpha/beta domain and a small alpha-helical domain and harbors three catalytic residues (Ser71, Lys74, and Tyr160) in the cavity at the domain interface, similarly to other family VIII carboxylesterases. Comparison of the structures of EstSRT1 and EstU1, a family VIII carboxylesterase with no hydrolytic activity toward bulky oxyimino cephalosporins, revealed that EstSRT1 has a smaller active site, despite its extended substrate range. The B-factors of the active site segments that could potentially contact with the oxyimino groups and the R2 side chains of oxyimino cephalosporins are higher in EstSRT1 than in EstU1, thus suggesting the role of the active site's structural flexibility in the extension of EstSRT1's substrate spectrum. (C) 2016 Elsevier Inc. All rights reserved.
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ISSN
- 0006-291X
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/1435
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DOI
- 10.1016/j.bbrc.2016.08.031
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Bibliographic Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.478, no.2, pp.818 - 824, 2016
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Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
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Subject
- C BETA-LACTAMASES; EXTENDED-SPECTRUM; CLASSIFICATION; ENZYMES
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Keywords
- Family VIII carboxylesterases; EstSRT1; Crystal structure; Extended hydrolytic activity toward oxyimino cephalosporins; Flexibility of the active site
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Type
- Article
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Language
- English
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Document Type
- Article
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