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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-05

AUTHORS

Kaoru Kumazaki, Toshiki Kishimoto, Arata Furukawa, Hiroyuki Mori, Yoshiki Tanaka, Naoshi Dohmae, Ryuichiro Ishitani, Tomoya Tsukazaki, Osamu Nureki

ABSTRACT

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. More... »

PAGES

7299

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep07299

DOI

http://dx.doi.org/10.1038/srep07299

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017383571

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25466392


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