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

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.

SUBMITTER: Allen MD

PROVIDER: S-EPMC4661788 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature

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

Allen Mark D MD Christie Mary M Jones Peter P Porebski Benjamin T BT Roome Brendan B Freund Stefan M V SM Buckle Ashley M AM Bycroft Mark M Christ Daniel D

Protein engineering, design & selection : PEDS 20150415 10

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 ...[more]

PMID: 25877662

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