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

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

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2 Citations (Scopus)

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
Number of pages6
JournalProtein Engineering Design and Selection
Volume28
Issue number10
DOIs
Publication statusPublished - 2015

Cite this

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