溶解
大肠杆菌
生物
跨膜蛋白
伴侣(临床)
细菌
细菌细胞结构
蛋白质结构
溶解循环
微生物学
生物化学
遗传学
基因
病毒
医学
受体
病理
作者
Anna K. Orta,Nadia Riera,Yancheng E. Li,Shiho Tanaka,Hyun Gi Yun,Lada Klaić,William Clemons
出处
期刊:Science
[American Association for the Advancement of Science]
日期:2023-07-13
卷期号:381 (6654): eadg9091-eadg9091
被引量:42
标识
DOI:10.1126/science.adg9091
摘要
The historically important phage ΦX174 kills its host bacteria by encoding a 91-residue protein antibiotic called protein E. Using single-particle electron cryo-microscopy, we demonstrate that protein E bridges two bacterial proteins to form the transmembrane YES complex [MraY, protein E, sensitivity to lysis D (SlyD)]. Protein E inhibits peptidoglycan biosynthesis by obstructing the MraY active site leading to loss of lipid I production. We experimentally validate this result for two different viral species, providing a clear model for bacterial lysis and unifying previous experimental data. Additionally, we characterize the Escherichia coli MraY structure-revealing features of this essential enzyme-and the structure of the chaperone SlyD bound to a protein. Our structures provide insights into the mechanism of phage-mediated lysis and for structure-based design of phage therapeutics.
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