Crystal structure of the EnvZ periplasmic domain with CHAPS

• Published in: FEBS letters Vol. 591; no. 10; pp. 1419 - 1428
• Main Authors: Hwang, Eunha, Cheong, Hae‐Kap, Kim, Sang‐Yoon, Kwon, Ohsuk, Blain, Katherine Y., Choe, Senyon, Yeo, Kwon Joo, Jung, Yong Woo, Jeon, Young Ho, Cheong, Chaejoon
• Format: Journal Article
• Language: English
• Published: England 01-05-2017
• Subjects: Bacterial Outer Membrane Proteins - chemistry; Bacterial Outer Membrane Proteins - drug effects; Cholates - pharmacology; Cholic Acids - pharmacology; Circular Dichroism; Crystallography, X-Ray; Detergents - pharmacology; EnvZ; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - drug effects; Models, Molecular; Multienzyme Complexes - chemistry; Multienzyme Complexes - drug effects; periplasmic domain; Protein Domains - drug effects; Protein Folding - drug effects; Protein Structure, Secondary - drug effects; X‐ray crystallography; X-ray crystallography; EnvZ; periplasmic domain
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1002/1873-3468.12658

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.