周质间隙
细菌外膜
分子机器
膜
内膜
生物
叶绿体
功能(生物学)
大肠杆菌
整体膜蛋白
膜蛋白
生物物理学
生物化学
细胞生物学
遗传学
基因
作者
Seokhee Kim,Juliana C. Malinverni,Piotr Sliz,Thomas J. Silhavy,Stephen C. Harrison,Daniel Kahne
出处
期刊:Science
[American Association for the Advancement of Science]
日期:2007-08-16
卷期号:317 (5840): 961-964
被引量:356
标识
DOI:10.1126/science.1143993
摘要
Integral beta-barrel proteins are found in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria. The machine that assembles these proteins contains an integral membrane protein, called YaeT in Escherichia coli, which has one or more polypeptide transport-associated (POTRA) domains. The crystal structure of a periplasmic fragment of YaeT reveals the POTRA domain fold and suggests a model for how POTRA domains can bind different peptide sequences, as required for a machine that handles numerous beta-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine.
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