期刊
SCIENTIFIC REPORTS
卷 4, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/srep07299
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology (MEXT)
- JSPS/ MEXT KAKENHI [26119007, 26102532, 26291023, 25116705, 24227004, 13J08353]
- FIRST program
- PRESTO, JST
- MEXT
- Astellas Foundation for Research on Metabolic Disorders
- Sumitomo Foundation
- Grants-in-Aid for Scientific Research [26102532, 13J08353, 24117003, 22117007, 26119007, 26291023, 25116705] Funding Source: KAKEN
Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane protein chaperone in cooperation with the Sec translocon and as an independent insertase for membrane proteins. In Gram-negative bacteria, the transmembrane and periplasmic regions of YidC interact with the Sec proteins, forming a multi-protein complex for Sec-dependent membrane protein integration. Here, we report the crystal structure of full-length Escherichia coli YidC. The structure reveals that a hydrophilic groove, formed by five transmembrane helices, is a conserved structural feature of YidC, as compared to the previous YidC structure from Bacillus halodurans, which lacks a periplasmic domain. Structural mapping of the substrate or Sec protein-contact sites suggested the importance of the groove for the YidC functions as a chaperone and an insertase, and provided structural insight into the multi-protein complex.
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