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

• Kumazaki, Kaoru

• Kishimoto, Toshiki

• Furukawa, Arata

• Mori, Hiroyuki

• Tanaka, Yoshiki

• Dohmae, Naoshi

• Ishitani, Ryuichiro

• Tsukazaki, Tomoya

• Nureki, Osamu

Bibliographic Information

Other Title

• Crystal Structure of Escherichia coli YidC, Membrane Protein Chaperone and Insertase

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.

Journal

• SCIENTIFIC REPORTS

  SCIENTIFIC REPORTS 4 7299-, 2014-12-03

  Macmillan Publishers

Keywords

• Structural biology
• X-ray crystallography

Details

• CRID: 1050295834376169472
• NII Article ID: 120005716851
• NII Book ID: AA10703873
• ISSN: 20452322
• DOI: 10.1038/srep07299
• HANDLE: 10061/9861
• Web Site: https://naist.repo.nii.ac.jp/records/9115
• Web Site: https://www.nature.com/articles/srep07299.pdf
• Web Site: https://www.nature.com/articles/srep07299
• Text Lang: en
• Article Type: journal article
• Data Source:
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  • Crossref
  • CiNii Articles
  • KAKEN