The crystal structure Escherichia coli Spy

Title
The crystal structure Escherichia coli Spy
Author(s)
권은주[권은주]김동영Carol A. Gross[Carol A. Gross]John D. Gross[John D. Gross]김경규[김경규]
Keywords
ENVELOPE STRESS-RESPONSE; PROTEIN; SYSTEM; CPXP; ELECTROSTATICS; MEMBRANE; SOFTWARE; COPPER; SUITE; DEGP
Issue Date
201011
Publisher
WILEY-BLACKWELL
Citation
PROTEIN SCIENCE, v.19, no.11, pp.2252 - 2259
Abstract
Escherichia coli spheroplast protein y (EcSpy) is a small periplasmic protein that is homologous with CpxP, an inhibitor of the extracytoplasmic stress reponse. 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 alpha-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, stablizing 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.
URI
http://hdl.handle.net/YU.REPOSITORY/23375http://dx.doi.org/10.1002/pro.489
ISSN
0961-8368
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약학대학 > 약학부 > Articles
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