Computational redesign of the lipid-facing surface of the outer membrane protein OmpA
Models, Molecular
0301 basic medicine
Protein Folding
0303 health sciences
Proline
Molecular Sequence Data
Computational Biology
Flow Cytometry
Lipids
Fluorescence
Protein Structure, Secondary
Recombinant Proteins
03 medical and health sciences
Escherichia coli
Electrophoresis, Polyacrylamide Gel
Mutant Proteins
Amino Acid Sequence
Sequence Alignment
Bacterial Outer Membrane Proteins
DOI:
10.1073/pnas.1501836112
Publication Date:
2015-07-22T02:10:15Z
AUTHORS (3)
ABSTRACT
Significance
The ability to construct novel proteins from basic principles of molecular structure is the fundamental goal of protein design. This is particularly challenging in the case of the β-barrel outer membrane proteins, where our understanding of the rules governing structure and function lags behind that of other classes of proteins. Here, we took a step toward understanding β-barrel membrane protein architecture by focusing on the outward-facing amino acid positions that contact the cell membrane. We replaced the membrane-facing surface of OmpA with new surfaces designed to resemble natural β-barrel surfaces. We were able to design versions of OmpA with mutations at about two-thirds of all surface positions, indicating that β-barrel membrane protein surface design is achievable.
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CITATIONS (30)
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