Co-translational translocon insertion and topogenesis of bacterial membrane proteins

Author(s):  
Evan Mercier
1972 ◽  
Vol 10 (1) ◽  
pp. 137-152 ◽  
Author(s):  
Charles Moldow ◽  
John Robertson ◽  
Lawrence Rothfield

2010 ◽  
Vol 43 (1) ◽  
pp. 58-63 ◽  
Author(s):  
Zbigniew Pietras ◽  
Hong-Ting Lin ◽  
Sachin Surade ◽  
Ben Luisi ◽  
Orla Slattery ◽  
...  

The use of an organic solvent-based gel prepared from polyethylene oxide and a polyvinyl alcohol hydrogel for protein crystallization was investigated. The preparation, properties and application of the gels for protein crystallization are described, and the advantages and limitations of the approach are discussed. The gels are compared with agar, which is a popular aqueous gel used for protein crystallization. The growth behaviour and diffraction quality of crystals prepared in these gel media were evaluated for two model soluble proteins, thaumatin and lysozyme, and for two bacterial membrane proteins, TolC and AcrB.


2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Thomas Harkey ◽  
Vivek Govind Kumar ◽  
Jeevapani Hettige ◽  
Seyed Hamid Tabari ◽  
Kalyan Immadisetty ◽  
...  

Abstract YidC, a bacterial member of the YidC/Alb3/Oxa1 insertase family, mediates membrane protein assembly and insertion. Cytoplasmic loops are known to have functional significance in membrane proteins such as YidC. Employing microsecond-level molecular dynamics (MD) simulations, we show that the crystallographically unresolved C2 loop plays a crucial role in the structural dynamics of Bacillus halodurans YidC2. We have modeled the C2 loop and used all- atom MD simulations to investigate the structural dynamics of YidC2 in its apo form, both with and without the C2 loop. The C2 loop was found to stabilize the entire protein and particularly the C1 region. C2 was also found to stabilize the alpha-helical character of the C-terminal region. Interestingly, the highly polar or charged lipid head groups of the simulated membranes were found to interact with and stabilize the C2 loop. These findings demonstrate that the crystallographically unresolved loops of membrane proteins could be important for the stabilization of the protein despite the apparent lack of structure, which could be due to the absence of the relevant lipids to stabilize them in crystallographic conditions.


Sign in / Sign up

Export Citation Format

Share Document