Summary for 5XGA
| Entry DOI | 10.2210/pdb5xga/pdb |
| Descriptor | Osmolarity sensor protein EnvZ, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, ACETIC ACID, ... (4 entities in total) |
| Functional Keywords | histidine kinase, envz, transferase |
| Biological source | Escherichia coli (strain K12) |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P0AEJ4 |
| Total number of polymer chains | 1 |
| Total formula weight | 15646.12 |
| Authors | Hwang, E.,Cheong, H.K.,Jeon, Y.H.,Cheong, C. (deposition date: 2017-04-13, release date: 2017-07-19, Last modification date: 2024-03-27) |
| Primary citation | Hwang, E.,Cheong, H.K.,Kim, S.Y.,Kwon, O.,Blain, K.Y.,Choe, S.,Yeo, K.J.,Jung, Y.W.,Jeon, Y.H.,Cheong, C. Crystal structure of the EnvZ periplasmic domain with CHAPS. FEBS Lett., 591:1419-1428, 2017 Cited by PubMed Abstract: 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. PubMed: 28423182DOI: 10.1002/1873-3468.12658 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.951 Å) |
Structure validation
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