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Title: A YidC-like Protein in the Archaeal Plasma Membrane

Authors:
; ; ; ;  [1]
  1. UC
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NIHOTHER
OSTI Identifier:
1259889
Resource Type:
Journal Article
Resource Relation:
Journal Name: Structure; Journal Volume: 23; Journal Issue: 9
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Borowska, Marta T., Dominik, Pawel K., Anghel, S. Andrei, Kossiakoff, Anthony A., and Keenan, Robert J.. A YidC-like Protein in the Archaeal Plasma Membrane. United States: N. p., 2016. Web. doi:10.1016/j.str.2015.06.025.
Borowska, Marta T., Dominik, Pawel K., Anghel, S. Andrei, Kossiakoff, Anthony A., & Keenan, Robert J.. A YidC-like Protein in the Archaeal Plasma Membrane. United States. doi:10.1016/j.str.2015.06.025.
Borowska, Marta T., Dominik, Pawel K., Anghel, S. Andrei, Kossiakoff, Anthony A., and Keenan, Robert J.. 2016. "A YidC-like Protein in the Archaeal Plasma Membrane". United States. doi:10.1016/j.str.2015.06.025.
@article{osti_1259889,
title = {A YidC-like Protein in the Archaeal Plasma Membrane},
author = {Borowska, Marta T. and Dominik, Pawel K. and Anghel, S. Andrei and Kossiakoff, Anthony A. and Keenan, Robert J.},
abstractNote = {},
doi = {10.1016/j.str.2015.06.025},
journal = {Structure},
number = 9,
volume = 23,
place = {United States},
year = 2016,
month = 6
}
  • Cited by 5
  • Cited by 5
  • The overproduction, purification, crystallization and preliminary crystallographic studies of the native and selenomethionine-labelled P1 domain are reported here as a first step towards the elucidation of the molecular mechanism of YidC as a membrane-protein insertase. In Escherichia coli, the biogenesis of inner membrane proteins (IMPs) requires targeting and insertion factors such as the signal recognition particle (SRP) and the Sec translocon. Recent studies have identified YidC as a novel and essential component involved in membrane insertion of IMPs both in conjunction with the Sec translocon and as a separate entity. E. coli YidC is a member of the YidC (inmore » bacteria)/Oxa1 (in mitochondria)/Alb3 (in chloroplasts) protein family and contains six transmembrane segments and a very large periplasmic domain P1. The overproduction, purification, crystallization and preliminary crystallographic studies of the native and selenomethionine-labelled P1 domain are reported here as a first step towards the elucidation of the molecular mechanism of YidC as a membrane-protein insertase.« less
  • YidC, a membrane-protein chaperone/insertase from B. halodurans, was expressed, purified and crystallized in the lipidic cubic phase. An X-ray diffraction data set was collected to 2.4 Å resolution. YidC, a member of the YidC/Oxa1/Alb3 family, inserts proteins into the membrane and facilitates membrane-protein folding in bacteria. YidC plays key roles in both Sec-mediated integration and Sec-independent insertion of membrane proteins. Here, Bacillus halodurans YidC2, which has five transmembrane helices conserved among the other family members, was identified as a target protein for structure determination by a fluorescent size-exclusion chromatography analysis. The protein was overexpressed, purified and crystallized in the lipidicmore » cubic phase. The crystals diffracted X-rays to 2.4 Å resolution and belonged to space group P2{sub 1}, with unit-cell parameters a = 43.9, b = 60.6, c = 58.9 Å, β = 100.3°. The experimental phases were determined by the multiwavelength anomalous diffraction method using a mercury-derivatized crystal.« less