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- W1532149086 abstract "Escherichia coli spheroplast protein y (EcSpy) is a small periplasmic protein that is homologous with CpxP, an inhibitor of the extracytoplasmic stress response. Stress conditions such as spheroplast formation induce the expression of Spy via the Cpx or the Bae two-component systems in E. coli, though the function of Spy is unknown. Here, we report the crystal structure of EcSpy, which reveals a long kinked hairpin-like structure of four α-helices that form an antiparallel dimer. The dimer contains a curved oval shape with a highly positively charged concave surface that may function as a ligand binding site. Sequence analysis reveals that Spy is highly conserved over the Enterobacteriaceae family. Notably, three conserved regions that contain identical residues and two LTxxQ motifs are placed at the horizontal end of the dimer structure, stabilizing the overall fold. CpxP also contains the conserved sequence motifs and has a predicted secondary structure similar to Spy, suggesting that Spy and CpxP likely share the same fold." @default.
- W1532149086 created "2016-06-24" @default.
- W1532149086 creator A5033627049 @default.
- W1532149086 creator A5040138828 @default.
- W1532149086 creator A5058141241 @default.
- W1532149086 creator A5061964396 @default.
- W1532149086 creator A5063595248 @default.
- W1532149086 date "2010-09-24" @default.
- W1532149086 modified "2023-10-07" @default.
- W1532149086 title "The crystal structure<i>Escherichia coli</i>Spy" @default.
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- W1532149086 doi "https://doi.org/10.1002/pro.489" @default.
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