Inhibition of phospho-MurNAc-pentapeptide translocase (MraY) by nucleoside natural product antibiotics, bacteriophage φX174 lysis protein E, and cationic antibacterial peptides
Inhibition of phospho-MurNAc-pentapeptide translocase (MraY) by nucleoside natural product antibiotics, bacteriophage φX174 lysis protein E, and cationic antibacterial peptides
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DOI：
10.1016/j.bmc.2016.03.018
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发表时间：
2016-12-15
影响因子：
3.5
通讯作者：
Jamshidi, Shirin
中科院分区：
文献类型：
--
作者：
Bugg, Timothy D. H.;Rodolis, Maria T.;Jamshidi, Shirin
本文综述了近年来对转位酶mray及其相关的磷酸化GlcNAc转移酶WECA和TAG的抑制作用的研究进展，并从Aquifex aeolicus mray的结构上深入探讨了这类膜蛋白的抑制和催化机制。最近的研究也发现了大肠杆菌mray中的一个蛋白质-蛋白质相互作用位点，它是噬菌体Phi x174裂解蛋白E的靶点，也是N端或C端含有Arg-Trp的阳离子抗菌肽的靶点。(C)2016爱思唯尔有限公司。保留所有权利。
This review covers recent developments in the inhibition of translocase MraY and related phospho-GlcNAc transferases WecA and Tag, and insight into the inhibition and catalytic mechanism of this class of integral membrane proteins from the structure of Aquifex aeolicus MraY. Recent studies have also identified a protein-protein interaction site in Escherichia coli MraY, that is targeted by bacteriophage phi X174 lysis protein E, and also by cationic antimicrobial peptides containing Arg-Trp close to their N- or C-termini. (C) 2016 Elsevier Ltd. All rights reserved.