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Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase

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 prot...

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Detalles Bibliográficos
Autores principales: Kumazaki, Kaoru, Kishimoto, Toshiki, Furukawa, Arata, Mori, Hiroyuki, Tanaka, Yoshiki, Dohmae, Naoshi, Ishitani, Ryuichiro, Tsukazaki, Tomoya, Nureki, Osamu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4252904/
https://www.ncbi.nlm.nih.gov/pubmed/25466392
http://dx.doi.org/10.1038/srep07299
Descripción
Sumario: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.