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

Sci Rep. 2014 Dec 3;4:7299. doi: 10.1038/srep07299.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / metabolism
  • Crystallography, X-Ray / methods
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Membrane Proteins / chemistry*
  • Membrane Transport Proteins / chemistry*
  • Molecular Chaperones / chemistry*
  • Protein Structure, Secondary

Substances

  • Escherichia coli Proteins
  • Membrane Proteins
  • Membrane Transport Proteins
  • Molecular Chaperones
  • YIDC protein, E coli

Associated data

  • PDB/3WVF