Proteopedia entry: Structure of complex membrane proteins solved using cryo‐ electron microscopy

2021 ◽  
Author(s):  
R. Jeremy Johnson ◽  
Grace Bassler ◽  
Emma Harris ◽  
Ryan Heumann ◽  
Abby Hillan ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Membrane Proteins ◽  
Cryo Electron Microscopy ◽  
Complex Membrane

scholarly journals Cryo-electron Microscopy of Membrane Proteins

2013 ◽  
pp. 325-341 ◽  
Author(s):  
Kenneth N. Goldie ◽  
Priyanka Abeyrathne ◽  
Fabian Kebbel ◽  
Mohamed Chami ◽  
Philippe Ringler ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Membrane Proteins ◽  
Cryo Electron Microscopy

scholarly journals Structure of the posttranslational Sec protein-translocation channel complex from yeast

Science ◽  
2018 ◽  
Vol 363 (6422) ◽  
pp. 84-87 ◽  
Author(s):  
Samuel Itskanov ◽  
Eunyong Park
Keyword(s):  
Electron Microscopy ◽  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Binding Sites ◽  
Protein Translocation ◽  
Secretory Proteins ◽  
Conducting Channel ◽  
Cryo Electron Microscopy ◽  
Lateral Gate

The Sec61 protein-conducting channel mediates transport of many proteins, such as secretory proteins, across the endoplasmic reticulum (ER) membrane during or after translation. Posttranslational transport is enabled by two additional membrane proteins associated with the channel, Sec63 and Sec62, but its mechanism is poorly understood. We determined a structure of the Sec complex (Sec61-Sec63-Sec71-Sec72) from Saccharomyces cerevisiae by cryo–electron microscopy (cryo-EM). The structure shows that Sec63 tightly associates with Sec61 through interactions in cytosolic, transmembrane, and ER-luminal domains, prying open Sec61’s lateral gate and translocation pore and thus activating the channel for substrate engagement. Furthermore, Sec63 optimally positions binding sites for cytosolic and luminal chaperones in the complex to enable efficient polypeptide translocation. Our study provides mechanistic insights into eukaryotic posttranslational protein translocation.

scholarly journals Cryo-electron microscopy of membrane proteins

Methods ◽  
2018 ◽  
Vol 147 ◽  
pp. 176-186 ◽  
Author(s):  
Nopnithi Thonghin ◽  
Vasileios Kargas ◽  
Jack Clews ◽  
Robert C. Ford
Keyword(s):  
Electron Microscopy ◽  
Membrane Proteins ◽  
Cryo Electron Microscopy

Characterization of Membrane Proteins Using Cryo-Electron Microscopy

2018 ◽  
Vol 94 (1) ◽  
pp. e72
Author(s):  
Vanessa Carvalho ◽  
Joachim W. Pronk ◽  
Andreas H. Engel
Keyword(s):  
Electron Microscopy ◽  
Membrane Proteins ◽  
Cryo Electron Microscopy

scholarly journals Cryo-Electron Microscopy of Potassium Channel Membrane Proteins

2014 ◽  
Vol 20 (S3) ◽  
pp. 1206-1207
Author(s):  
Julia Kowal ◽  
Sebastian Scherer ◽  
Kushal Sejwal ◽  
Mohamed Chami ◽  
Paul Baumgartner ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Membrane Proteins ◽  
Potassium Channel ◽  
Cryo Electron Microscopy

scholarly journals The structure of an injectisome export gate demonstrates conservation of architecture in the core export gate between flagellar and virulence type three secretion systems

2019 ◽  
Author(s):  
Steven Johnson ◽  
Lucas Kuhlen ◽  
Justin C. Deme ◽  
Patrizia Abrusci ◽  
Susan M. Lea
Keyword(s):  
Electron Microscopy ◽  
Membrane Proteins ◽  
Complex Analysis ◽  
Secretion Systems ◽  
Core Complex ◽  
The Core ◽  
Cryo Electron Microscopy ◽  
Equivalent Complex ◽  
Type Three Secretion ◽  
Resolution Structure

AbstractExport of proteins through type three secretion systems (T3SS) is critical for motility and virulence of many major bacterial pathogens. Proteins are exported though a genetically defined export gate complex consisting of three proteins. We have recently shown at 4.2 Å that the flagellar complex of these three putative membrane proteins (FliPQR in flagellar systems, SctRST in virulence systems) assemble into an extra-membrane helical assembly that likely seeds correct assembly of the rod above. Here we present the structure of an equivalent complex from the more fragile Shigella virulence system at 3.5 Å by cryo-electron microscopy. This higher resolution structure reveals further detail and confirms the prediction of structural conservation in this core complex. Analysis of particle heterogeneity also reveals details of how the SctS/FliQ subunits sequentially assemble in the complex.

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