Structural highlights
Function
YIDC_ECOUT
Publication Abstract from PubMed
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.
Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase.,Kumazaki K, Kishimoto T, Furukawa A, Mori H, Tanaka Y, Dohmae N, Ishitani R, Tsukazaki T, Nureki O Sci Rep. 2014 Dec 3;4:7299. doi: 10.1038/srep07299. PMID:25466392[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kumazaki K, Kishimoto T, Furukawa A, Mori H, Tanaka Y, Dohmae N, Ishitani R, Tsukazaki T, Nureki O. Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase. Sci Rep. 2014 Dec 3;4:7299. doi: 10.1038/srep07299. PMID:25466392 doi:http://dx.doi.org/10.1038/srep07299
