The crystal structure of the periplasmic domain of Vibrio parahaemolyticus CpxA

Title
The crystal structure of the periplasmic domain of Vibrio parahaemolyticus CpxA
Author(s)
권은주[권은주]김동영Tri Duc Ngo[Tri Duc Ngo]Carol A. Gross[Carol A. Gross]John D. Gross[John D. Gross]김경규[김경규]
Keywords
SIGNAL-TRANSDUCTION PATHWAY; ENVELOPE STRESS RESPONSES; ESCHERICHIA-COLI; 2-COMPONENT SYSTEM; MACROMOLECULAR STRUCTURES; PROTEIN; ACTIVATION; SENSOR; MODEL; DEGP
Issue Date
201209
Publisher
WILEY-BLACKWELL
Citation
PROTEIN SCIENCE, v.21, no.9, pp.1334 - 1343
Abstract
The Cpx two-component system of Gram-negative bacteria senses extracytoplasmic stresses using the histidine kinase CpxA, a membrane-bound sensor, and controls the transcription of the genes involved in stress response by the cytosolic response regulator CpxR, which is activated by the phosphorelay from CpxA. CpxP, a CpxA-associated protein, also plays an important role in the regulation of the Cpx system by inhibiting the autophosphorylation of CpxA. Although the stress signals and physiological roles of the Cpx system have been extensively studied, the lack of structural information has limited the understanding of the detailed mechanism of ligand binding and regulation of CpxA. In this study, we solved the crystal structure of the periplasmic domain of Vibrio parahaemolyticus CpxA (VpCpxA-peri) to a resolution of 2.1 angstrom and investigated its interaction with CpxP. VpCpxA-peri has a globular Per-ARNT-SIM (PAS) domain and a protruded C-terminal tail, which may be required for ligand sensing and CpxP binding, respectively. The direct interaction of the PAS core of VpCpxA-peri with VpCpxP was not detected by NMR, suggesting that the C-terminal tail or other factors, such as the membrane environment, are necessary for the binding of CpxA to CpxP.
URI
http://hdl.handle.net/YU.REPOSITORY/27300http://dx.doi.org/10.1002/pro.2120
ISSN
0961-8368
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약학대학 > 약학부 > Articles
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