Structure and Functional Aspects of the bacterial bifunctional transglycosylase PBP1b from E. coli and Binding Interactions with Moenomycin
Structure and Functional Aspects of the bacterial bifunctional transglycosylase PBP1b from E. coli and Binding Interactions with Moenomycin
本院覽號
28A-970718
公告日期
智財權狀態
美國臨時案已申請、美國放棄申請、PCT已申請、美國9,890,111 B2放棄維護
摘要
The invention relates to the crystal structure of the full-length bacterial bifunctional tranasglycosylase PBP1b from E. coli, in complex with its inhibitor Moenomycin. PBP1b from E. coli is a bifunctional enzyme containing both glycosyltransferase and transpeptidase acitivity (class A penicillin-binding protein). The sequence of PBP1b is composed of an N-terminal single-spanning transmembrane (TM) helix and a functionally-unknown insertion followed by the glycosyltransferase (TG) domain and the C-terminal transpeptidase (TP) domain. A three-dimensional structure of the membrane-bound enzyme tranasglycosylase was determined by X-ray crystallography.
技術優勢
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應用範圍
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創作人
Chi-Huey Wong, Che Ma
Structure and Functional Aspects of the bacterial bifunctional transglycosylase PBP1b from E. coli and Binding Interactions with Moenomycin
