8번째 carboxylesterase family에 속하는 EstU1의 beta-lactamase 활성에 대한 구조기반 연구

Title
8번째 carboxylesterase family에 속하는 EstU1의 beta-lactamase 활성에 대한 구조기반 연구
Alternative Title
Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase
Author(s)
안영준; 정창숙; 김민규; jeong; 이현숙; 강성균; 이정현; 차선신
KIOST Author(s)
Young, Jun An(안영준)Lee, Hyun Sook(이현숙)Kang, Sung Gyun(강성균)Lee, Jung Hyun(이정현)
Alternative Author(s)
안영준; 정창숙; 김민규; 이현숙; 강성균; 이정현; 차선신
Publication Year
2013-05-03
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.
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/27095
Bibliographic Citation
2013년 한국미생물학회 국제학술대회, pp.267, 2013
Publisher
한국미생물학회
Type
Conference
Language
English
Publisher
한국미생물학회
Related Researcher
Research Interests

marine biotechnology,molecular microbiology,해양생명공학,분자미생물학

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