3WVF

Crystal structure of YidC from Escherichia coli

Summary for 3WVF

• Entry DOI: 10.2210/pdb3wvf/pdb
• Descriptor: Membrane protein insertase YidC (1 entity in total)
• Functional Keywords: alpha helical, chaperone
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane ; Multi-pass membrane protein : Q1R4M9
• Total number of polymer chains: 2
• Total formula weight: 123745.41

Authors

Kumazaki, K.,Tsukazaki, T.,Kishimoto, T.,Ishitani, R.,Nureki, O. (deposition date: 2014-05-20, release date: 2014-12-17, Last modification date: 2023-11-08)

Primary citation

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, 4:7299-7299, 2014

PubMed 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.

PubMed: 25466392
DOI: 10.1038/srep07299

Experimental method

X-RAY DIFFRACTION (3.2 Å)