周质间隙
肽聚糖
细胞生物学
细菌细胞结构
低温电子显微
细胞分裂
脂质Ⅱ
生物
化学
大肠杆菌
细胞
细菌
生物化学
细胞壁
遗传学
基因
作者
Lisa Käshammer,F. van den Ent,Magnus Jeffery,Nicolas L Jean,Victoria L. Hale,Jan Löwe
出处
期刊:Nature microbiology
日期:2023-05-01
卷期号:8 (6): 1149-1159
被引量:18
标识
DOI:10.1038/s41564-023-01368-0
摘要
In most bacteria, cell division relies on the synthesis of new cell wall material by the multiprotein divisome complex. Thus, at the core of the divisome are the transglycosylase FtsW, which synthesises peptidoglycan strands from its substrate Lipid II, and the transpeptidase FtsI that cross-links these strands to form a mesh, shaping and protecting the bacterial cell. The FtsQ–FtsB–FtsL trimeric complex interacts with the FtsWI complex and is involved in regulating its enzymatic activities; however, the structure of this pentameric complex is unknown. Here, we present the cryogenic electron microscopy structure of the FtsWIQBL complex from Pseudomonas aeruginosa at 3.7 Å resolution. Our work reveals intricate structural details, including an extended coiled coil formed by FtsL and FtsB and the periplasmic interaction site between FtsL and FtsI. Our structure explains the consequences of previously reported mutations and we postulate a possible activation mechanism involving a large conformational change in the periplasmic domain. As FtsWIQBL is central to the divisome, our structure is foundational for the design of future experiments elucidating the precise mechanism of bacterial cell division, an important antibiotic target. The cryogenic electron microscopy structure of the Pseudomonas aeruginosa cell division complex and antibiotic drug target, FtsWIQBL, suggests a possible activation mechanism.
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