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Crystal structure of the EnvZ periplasmic domain with CHAPS
Author(s) -
Hwang Eunha,
Cheong HaeKap,
Kim SangYoon,
Kwon Ohsuk,
Blain Katherine Y.,
Choe Senyon,
Yeo Kwon Joo,
Jung Yong Woo,
Jeon Young Ho,
Cheong Chaejoon
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12658
Subject(s) - chaps , periplasmic space , chemistry , crystal structure , crystallography , escherichia coli , biochemistry , biophysics , biology , gene , enzyme
Bacteria sense and respond to osmolarity through the EnvZ‐OmpR two‐component system. The structure of the periplasmic sensor domain of EnvZ (EnvZ‐PD) is not available yet. Here, we present the crystal structure of EnvZ‐PD in the presence of CHAPS detergent. The structure of EnvZ‐PD shows similar folding topology to the PDC domains of PhoQ, DcuS, and CitA, but distinct orientations of helices and β‐hairpin structures. The CD and NMR spectra of EnvZ‐PD in the presence of cholate, a major component of bile salts, are similar to those with CHAPS. Chemical cross‐linking shows that the dimerization of EnvZ‐PD is significantly inhibited by the CHAPS and cholate. Together with β‐galactosidase assay, these results suggest that bile salts may affect the EnvZ structure and function in Escherichia coli .