Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis.
We have previously reported a phage display method for the identification of protein domains on a genome-wide scale (shotgun proteolysis). Here we present the solution structure of a fragment of the Escherichia coli membrane protein yrfF, as identified by shotgun proteolysis, and determined by NMR spectroscopy. Despite the absence of computational predictions, the fragment formed a well-defined beta-barrel structure, distantly falling within the OB-fold classification. Our results highlight the potential of high-throughput experimental approaches for the identification of protein domains for structural studies.
|Authors||Allen, M. D.; Christie, M.; Jones, P.; Porebski, B. T.; Roome, B.; Freund, S. M.; Buckle, A. M.; Bycroft, M.; Christ, D.;|
|Publisher Name||PROTEIN ENG DES SEL|
|Published Date||2015-10-01 00:00:00|