Crystal structure of EstSRT1, a family VIII carboxylesterase displaying hydrolytic activity toward oxyimino cephalosporins SCIE SCOPUS

Cited 9 time in WEB OF SCIENCE Cited 9 time in Scopus
Title
Crystal structure of EstSRT1, a family VIII carboxylesterase displaying hydrolytic activity toward oxyimino cephalosporins
Author(s)
Cha, Sun-Shin; An, Young Jun
KIOST Author(s)
An, Young Jun(안영준)
Alternative Author(s)
안영준
Publication Year
2016-09-16
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.
ISSN
0006-291X
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/1435
DOI
10.1016/j.bbrc.2016.08.031
Bibliographic Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.478, no.2, pp.818 - 824, 2016
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Subject
C BETA-LACTAMASES; EXTENDED-SPECTRUM; CLASSIFICATION; ENZYMES
Keywords
Family VIII carboxylesterases; EstSRT1; Crystal structure; Extended hydrolytic activity toward oxyimino cephalosporins; Flexibility of the active site
Type
Article
Language
English
Document Type
Article
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