Structural highlights
Function
[ENVZ_ECOLI] Member of the two-component regulatory system EnvZ/OmpR involved in the regulation of osmoregulation (genes ompF and ompC). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals.
Publication Abstract from PubMed
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 beta-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 beta-galactosidase assay, these results suggest that bile salts may affect the EnvZ structure and function in Escherichia coli.
Crystal structure of the EnvZ periplasmic domain with CHAPS.,Hwang E, Cheong HK, Kim SY, Kwon O, Blain KY, Choe S, Yeo KJ, Jung YW, Jeon YH, Cheong C FEBS Lett. 2017 May;591(10):1419-1428. doi: 10.1002/1873-3468.12658. Epub 2017, May 9. PMID:28423182[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hwang E, Cheong HK, Kim SY, Kwon O, Blain KY, Choe S, Yeo KJ, Jung YW, Jeon YH, Cheong C. Crystal structure of the EnvZ periplasmic domain with CHAPS. FEBS Lett. 2017 May;591(10):1419-1428. doi: 10.1002/1873-3468.12658. Epub 2017, May 9. PMID:28423182 doi:http://dx.doi.org/10.1002/1873-3468.12658
