TY - JOUR
T1 - Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis
AU - Allen, Mark D.
AU - Christie, Mary
AU - Jones, Peter
AU - Porebski, Benjamin T.
AU - Roome, Brendan
AU - Freund, Stefan M. V.
AU - Buckle, Ashley M.
AU - Bycroft, Mark
AU - Christ, Daniel
PY - 2015/10/1
Y1 - 2015/10/1
N2 - 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.
AB - 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.
U2 - 10.1093/protein/gzv021
DO - 10.1093/protein/gzv021
M3 - Article
SN - 1741-0126
VL - 28
SP - 445
EP - 450
JO - Protein Engineering Design and Selection
JF - Protein Engineering Design and Selection
IS - 10
ER -