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.
Allen, M. D., Christie, M., Jones, P., Porebski, B. T., Roome, B., Freund, S. M. V., Buckle, A. M., Bycroft, M., & Christ, D. (2015). Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis. Protein Engineering Design and Selection, 28(10), 445 - 450. https://doi.org/10.1093/protein/gzv021