Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis

Mark D. Allen, Mary Christie, Peter Jones, Benjamin T. Porebski, Brendan Roome, Stefan M. V. Freund, Ashley M. Buckle, Mark Bycroft, Daniel Christ

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Abstract

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.
Original languageEnglish
Pages (from-to)445-450
JournalProtein Engineering Design and Selection
Volume28
Issue number10
Early online date15 Apr 2015
DOIs
Publication statusPublished - 1 Oct 2015
Externally publishedYes

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