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.;|
|Responsible Garvan Author|
|Publisher Name||PROTEIN ENGINEERING DESIGN & SELECTION|
|URL link to publisher's version||http://www.ncbi.nlm.nih.gov/pubmed/25877662|
|OpenAccess link to author's accepted manuscript version||https://publications.gimr.garvan.org.au/open-access/12771|