Folding of Circularly Permuted and Split Outer Membrane Protein F via Electrostatic Interactions with Terminal Residues

Biochemistry ◽  
2021 ◽  
Author(s):  
Jaewon Lee ◽  
Woon Ju Song
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Electrostatic Interactions ◽  
Protein F ◽  
Outer Membrane Protein F

Pseudomonas aeruginosa outer membrane protein F produced inEscherichia coli retains vaccine efficacy

1990 ◽  
Vol 20 (3) ◽  
pp. 171-175 ◽  
Author(s):  
Janice M. Matthews-Greer ◽  
Dawn E. Robertson ◽  
Linda B. Gilleland ◽  
Harry E. Gilleland
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Vaccine Efficacy ◽  
Inescherichia Coli ◽  
Protein F ◽  
Outer Membrane Protein F

scholarly journals High-yield membrane protein expression from E. coli using an engineered outer membrane protein F fusion

2013 ◽  
Vol 22 (4) ◽  
pp. 434-443 ◽  
Author(s):  
Pin-Chuan Su ◽  
William Si ◽  
Deidre L. Baker ◽  
Bryan W. Berger
Keyword(s):  
Membrane Protein ◽  
Protein Expression ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
High Yield ◽  
E Coli ◽  
Membrane Protein Expression ◽  
Protein F ◽  
Outer Membrane Protein F

Protein Ion Channels as Molecular Ratchets. Switchable Current Modulation in Outer Membrane Protein F Porin Induced by Millimolar La3+Ions

2012 ◽  
Vol 116 (11) ◽  
pp. 6537-6542 ◽  
Author(s):  
Carmina Verdiá-Báguena ◽  
María Queralt-Martín ◽  
Vicente M. Aguilella ◽  
Antonio Alcaraz
Keyword(s):  
Ion Channels ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Current Modulation ◽  
Protein F ◽  
Outer Membrane Protein F

scholarly journals Refolding of Escherichia coli outer membrane protein F in detergent creates LPS-free trimers and asymmetric dimers

2005 ◽  
Vol 392 (2) ◽  
pp. 375-381 ◽  
Author(s):  
Virak Visudtiphole ◽  
Matthew B. Thomas ◽  
David A. Chalton ◽  
Jeremy H. Lakey
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Single Molecule ◽  
Outer Membrane Protein ◽  
Structural Integrity ◽  
Protein F ◽  
Outer Membrane Protein F

The Escherichia coli OmpF (outer-membrane protein F; matrix porin) is a homotrimeric β-barrel and a member of the bacterial porin superfamily. It is the best characterized porin protein, but has resisted attempts to refold it efficiently in vitro. In the present paper, we report the discovery of detergent-based folding conditions, including dodecylglucoside, which can create pure samples of trimeric OmpF. Whereas outer membrane LPS (lipopolysaccharide) is clearly required for in vivo folding, the artificially refolded and LPS-free trimer has properties identical with those of the outer-membrane-derived form. Thus LPS is not required either for in vitro folding or for structural integrity. Dimeric forms of OmpF have been observed in vivo and are proposed to be folding intermediates. In vitro, dimers occur transiently in refolding of trimeric OmpF and, in the presence of dodecylmaltoside, pure dimer can be prepared. This form has less β-structure by CD and shows lower thermal stability than the trimer. Study of these proteins at the single-molecule level is possible because each OmpF subunit forms a distinct ion channel. Whereas each trimer contains three channels of equal conductance, each dimer always contains two distinct channel sizes. This provides clear evidence that the two otherwise identical monomers adopt different structures in the dimer and indicates that the asymmetric interaction, characteristic of C3 symmetry, is formed at the dimer stage. This asymmetric dimer may be generally relevant to the folding of oligomeric proteins with odd numbers of subunits such as aspartate transcarbamoylase.

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